Fc-conjugated C-type lectin receptors: Tools for understanding host-pathogen interactions.


Journal

Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028

Informations de publication

Date de publication:
03 2022
Historique:
received: 25 10 2021
accepted: 25 10 2021
pubmed: 29 10 2021
medline: 28 4 2022
entrez: 28 10 2021
Statut: ppublish

Résumé

The use of soluble fusion proteins of pattern recognition receptors (PRRs) used in the detection of exogenous and endogenous ligands has helped resolve the roles of PRRs in the innate immune response to pathogens, how they shape the adaptive immune response, and function in maintaining homeostasis. Using the immunoglobulin (Ig) crystallizable fragment (Fc) domain as a fusion partner, the PRR fusion proteins are soluble, stable, easily purified, have increased affinity due to the Fc homodimerization properties, and consequently have been used in a wide range of applications such as flow cytometry, screening of protein and glycan arrays, and immunofluorescent microscopy. This review will predominantly focus on the recognition of pathogens by the cell membrane-expressed glycan-binding proteins of the C-type lectin receptor (CLR) subgroup of PRRs. PRRs bind to conserved pathogen-associated molecular patterns (PAMPs), such as glycans, usually located within or on the outer surface of the pathogen. Significantly, many glycans structures are identical on both host and pathogen (e.g. the Lewis (Le) X glycan), allowing the use of Fc CLR fusion proteins with known endogenous and/or exogenous ligands as tools to identify pathogen structures that are able to interact with the immune system. Screens of highly purified pathogen-derived cell wall components have enabled identification of many unique PAMP structures recognized by CLRs. This review highlights studies using Fc CLR fusion proteins, with emphasis on the PAMPs found in fungi, bacteria, viruses, and parasites. The structure and unique features of the different CLR families is presented using examples from a broad range of microbes whenever possible.

Identifiants

pubmed: 34709692
doi: 10.1111/mmi.14837
doi:

Substances chimiques

Lectins, C-Type 0
Ligands 0
Pathogen-Associated Molecular Pattern Molecules 0
Receptors, Pattern Recognition 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

632-660

Subventions

Organisme : Medical Research Council
ID : MR/N006364/2
Pays : United Kingdom

Informations de copyright

© 2021 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.

Références

Achilli, S., Monteiro, J.T., Serna, S., Mayer-Lambertz, S., Thépaut, M., Le Roy, A. et al. (2020) TETRALEC, artificial tetrameric lectins: a tool to screen ligand and pathogen interactions. International Journal of Molecular Sciences, 21(15), 5290. Available from: https://doi.org/10.3390/ijms21155290
Akilov, O.E., Kasuboski, R.E., Carter, C.R. & McDowell, M.A. (2007) The role of mannose receptor during experimental leishmaniasis. Journal of Leukocyte Biology, 81(5), 1188-1196. Available from: https://doi.org/10.1189/jlb.0706439
Alain, B., Elsa, W.-R., Marie-Claire, B., Maryline, L., Christine, K.-H., Jean-François, H. et al. (2008) Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and fc-fusion proteins. Current Pharmaceutical Biotechnology, 9(6), 482-501.
Alvarez, C.P., Lasala, F., Carrillo, J., Muñiz, O., Corbí, A.L. & Delgado, R. (2002) C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. Journal of Virology, 76(13), 6841-6844.
Appelmelk, B.J., van Die, I., van Vliet, S.J., Vandenbroucke-Grauls, C.M.J.E., Geijtenbeek, T.B.H., van Kooyk, Y. (2003) Cutting Edge: carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells. The Journal of Immunology, 170(4), 1635-1639. Available from: https://doi.org/10.4049/jimmunol.170.4.1635
Arai, Y., Torigoe, S., Matsumaru, T., Yamasaki, S. & Fujimoto, Y. (2020) The key entity of a DCAR agonist, phosphatidylinositol mannoside Ac1PIM1: its synthesis and immunomodulatory function. Organic and Biomolecular Chemistry, 18(19), 3659-3663.
Balzarini, J. (2007) Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy. Nature Reviews Microbiology, 5(8), 583-597. Available from: https://doi.org/10.1038/nrmicro1707
Bloem, K., Vuist, I.M., van den Berk, M., Klaver, E.J., van Die, I., Knippels, L.M.J. et al. (2014) DCIR interacts with ligands from both endogenous and pathogenic origin. Immunology Letters, 158(1), 33-41. Available from: https://doi.org/10.1016/j.imlet.2013.11.007
Bloem, K., Vuist, I.M., van der Plas, A.-J., Knippels, L.M.J., Garssen, J., García-Vallejo, J.J. et al. (2013) Ligand binding and signaling of dendritic cell immunoreceptor (DCIR) is modulated by the glycosylation of the carbohydrate recognition domain. PLoS One, 8(6), e66266. Available from: https://doi.org/10.1371/journal.pone.0066266
Bode, K., Bujupi, F., Link, C., Hein, T., Zimmermann, S., Peiris, D. et al. (2019) Dectin-1 Binding to Annexins on Apoptotic Cells Induces Peripheral Immune Tolerance via NADPH Oxidase-2. Cell Reports, 29(13), 4435-4446.e4439. Available from: https://doi.org/10.1016/j.celrep.2019.11.086
Boesch, A.W., Brown, E.P., Cheng, H.D., Ofori, M.O., Normandin, E., Nigrovic, P.A. et al. (2014) Highly parallel characterization of IgG Fc binding interactions. mAbs, 6(4), 915-927. Available from: https://doi.org/10.4161/mabs.28808
Bongomin, F., Gago, S., Oladele, R.O. & Denning, D.W. (2017) Global and multi-national prevalence of fungal diseases-estimate precision. Journal of Fungi, 3(4), 57. Available from: https://doi.org/10.3390/jof3040057
Bonnardel, F., Mariethoz, J., Salentin, S., Robin, X., Schroeder, M., Perez, S. et al. (2018) UniLectin3D, a database of carbohydrate binding proteins with curated information on 3D structures and interacting ligands. Nucleic Acids Research, 47(D1), D1236-D1244. Available from: https://doi.org/10.1093/nar/gky832
Brown, G.D., Gordon, S. (2001) Immune recognition. A new receptor for beta-glucans. Nature, 413(6851), 36-37. Available from: https://doi.org/10.1038/35092620.
Brown, G.D., Willment, J.A. & Whitehead, L. (2018) C-type lectins in immunity and homeostasis. Nature Reviews Immunology, 18(6), 374-389. Available from: https://doi.org/10.1038/s41577-018-0004-8
Brown, S., Santa Maria, J.P. & Walker, S. (2013) Wall teichoic acids of gram-positive bacteria. Annual Review of Microbiology, 67(1), 313-336. Available from: https://doi.org/10.1146/annurev-micro-092412-155620
Brubaker, S.W., Bonham, K.S., Zanoni, I. & Kagan, J.C. (2015) Innate immune pattern recognition: a cell biological perspective. Annual Review of Immunology, 33(1), 257-290. Available from: https://doi.org/10.1146/annurev-immunol-032414-112240
Brzezicka, K., Echeverria, B., Serna, S., van Diepen, A., Hokke, C.H. & Reichardt, N.-C. (2015) Synthesis and microarray-assisted binding studies of core xylose and fucose containing N-glycans. ACS Chemical Biology, 10(5), 1290-1302. Available from: https://doi.org/10.1021/cb501023u
Brzezicka, K., Vogel, U., Serna, S., Johannssen, T., Lepenies, B. & Reichardt, N.-C. (2016) Influence of core β-1,2-xylosylation on glycoprotein recognition by murine C-type lectin receptors and its impact on dendritic cell targeting. ACS Chemical Biology, 11(8), 2347-2356. Available from: https://doi.org/10.1021/acschembio.6b00265
Campanero-Rhodes, M.A., Palma, A.S., Menéndez, M. & Solís, D. (2019) Microarray strategies for exploring bacterial surface glycans and their interactions with glycan-binding proteins. Frontiers in Microbiology, 10, 2909.
Campuzano, A. & Wormley, F.L. (2018) Innate immunity against cryptococcus, from recognition to elimination. Journal of Fungi, 4(1), 33. Available from: https://doi.org/10.3390/jof4010033
Cao, W., Calabro, V., Root, A., Yan, G., Lam, K., Olland, S. et al. (2009) Oligomerization is required for the activity of recombinant soluble LOX-1. The FEBS Journal, 276(17), 4909-4920. Available from: https://doi.org/10.1111/j.1742-4658.2009.07190.x
Cao, X. (2016) Self-regulation and cross-regulation of pattern-recognition receptor signalling in health and disease. Nature Reviews Immunology, 16(1), 35-50. Available from: https://doi.org/10.1038/nri.2015.8
Chaipan, C., Soilleux, E.J., Simpson, P., Hofmann, H., Gramberg, T., Marzi, A. et al. (2006) DC-SIGN and CLEC-2 mediate human immunodeficiency virus type 1 capture by platelets. Journal of Virology, 80(18), 8951-8960. Available from: https://doi.org/10.1128/JVI.00136-06
Chen, S.-T., Li, F.-J., Hsu, T.-Y., Liang, S.-M., Yeh, Y.-C., Liao, W.-Y. et al. (2017) CLEC5A is a critical receptor in innate immunity against Listeria infection. Nature Communications, 8(1), 299. Available from: https://doi.org/10.1038/s41467-017-00356-3
Chen, S.T., Lin, Y.L., Huang, M.T., Wu, M.F., Cheng, S.C., Lei, H.Y. et al. (2008) CLEC5A is critical for dengue-virus-induced lethal disease. Nature, 453(7195), 672-676. Available from: https://doi.org/10.1038/nature07013. Epub 2008 May 21. PMID: 18496526.
Cheng, A.C., Yang, K.Y., Chen, N.J., Hsu, T.L., Jou, R., Hsieh, S.L. et al. (2017) CLEC9A modulates macrophage-mediated neutrophil recruitment in response to heat-killed Mycobacterium tuberculosis H37Ra. PLoS One, 12(10), e0186780. Available from: https://doi.org/10.1371/journal.pone.0186780
Chiodo, F., Bruijns, S.C.M., Rodriguez, E., Li, R.J.E., Molinaro, A., Silipo, A. et al. (2020). Novel ACE2-independent carbohydrate-binding of SARS-CoV-2 spike protein to host lectins and lung microbiota. bioRxiv, 2020.2005.2013.092478.
Chowdhary, A., Sharma, C. & Meis, J.F. (2017) Candida auris: a rapidly emerging cause of hospital-acquired multidrug-resistant fungal infections globally. PLoS Pathogens, 13(5), e1006290. Available from: https://doi.org/10.1371/journal.ppat.1006290
Coakley, G. & Harris, N.L. (2020) Interactions between macrophages and helminths. Parasite Immunology, 42(7), e12717. Available from: https://doi.org/10.1111/pim.12717
Cvetkovic, J., Ilic, N., Gruden-Movsesijan, A., Tomic, S., Mitic, N., Pinelli, E. et al. (2020) DC-SIGN signalling induced by Trichinella spiralis products contributes to the tolerogenic signatures of human dendritic cells. Scientific Reports, 10(1), 20283. Available from: https://doi.org/10.1038/s41598-020-77497-x
Czajkowsky, D.M., Hu, J., Shao, Z. & Pleass, R.J. (2012) Fc-fusion proteins: new developments and future perspectives. EMBO Molecular Medicine, 4(10), 1015-1028. Available from: https://doi.org/10.1002/emmm.201201379
Daley, D., Mani, V.R., Mohan, N., Akkad, N., Ochi, A., Heindel, D.W. et al. (2017) Dectin 1 activation on macrophages by galectin 9 promotes pancreatic carcinoma and peritumoral immune tolerance. Nature Medicine, 23, 556-567. Available from: https://doi.org/10.1038/nm.4314
Dambuza, I.M. & Brown, G.D. (2015) C-type lectins in immunity: recent developments. Current Opinion in Immunology, 32, 21-27. Available from: https://doi.org/10.1016/j.coi.2014.12.002
Davis, C.W., Nguyen, H.-Y., Hanna, S.L., Sánchez, M.D., Doms, R.W. & Pierson, T.C. (2006) West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. Journal of Virology, 80(3), 1290-1301. Available from: https://doi.org/10.1128/JVI.80.3.1290-1301.2006
Decout, A., Silva-Gomes, S., Drocourt, D., Blattes, E., Rivière, M., Prandi, J. et al. (2018) Deciphering the molecular basis of mycobacteria and lipoglycan recognition by the C-type lectin Dectin-2. Scientific Reports, 8, 16840. Available from: https://doi.org/10.1038/s41598-018-35393-5
de Jong, M.A., Vriend, L.E., Theelen, B., Taylor, M.E., Fluitsma, D., Boekhout, T. et al. (2010) C-type lectin Langerin is a beta-glucan receptor on human Langerhans cells that recognizes opportunistic and pathogenic fungi. Molecular Immunology, 47(6), 1216-1225. Available from: https://doi.org/10.1016/j.molimm.2009.12.016
de Witte, L., Abt, M., Schneider-Schaulies, S., van Kooyk, Y. & Geijtenbeek, T.B.H. (2006) Measles virus targets DC-SIGN to enhance dendritic cell infection. Journal of Virology, 80(7), 3477-3486. Available from: https://doi.org/10.1128/JVI.80.7.3477-3486.2006
Del Pilar Jimenez, A.M., Viriyakosol, S., Walls, L., Datta, S.K., Kirkland, T., Heinsbroek, S.E. et al. (2008) Susceptibility to Coccidioides species in C57BL/6 mice is associated with expression of a truncated splice variant of Dectin-1 (Clec7a). Genes and Immunity, 9(4), 338-348. Available from: https://doi.org/10.1038/gene.2008.23
Denda-Nagai, K. & Irimura, T. (2016) MGL/CD301 as a unique C-type lectin expressed on dendritic cells and macrophages. In: Yamasaki, S. (Ed.) C-type lectin receptors in immunity. Springer Japan, pp. 165-178. Available from: https://doi.org/10.1007/978-4-431-56015-9_11
Drickamer, K. & Taylor, M.E. (2015) Recent insights into structures and functions of C-type lectins in the immune system. Current Opinion in Structural Biology, 34, 26-34. Available from: https://doi.org/10.1016/j.sbi.2015.06.003
Driessen, N.N., Ummels, R., Maaskant, J.J., Gurcha, S.S., Besra, G.S., Ainge, G.D. et al. (2009) Role of phosphatidylinositol mannosides in the interaction between mycobacteria and DC-SIGN. Infection and Immunity, 77(10), 4538-4547. Available from: https://doi.org/10.1128/IAI.01256-08
Drummond, R.A., Gaffen, S.L., Hise, A.G. & Brown, G.D. (2014) Innate defense against fungal pathogens. Cold Spring Harbor Perspectives in Medicine, 5(6), a019620.
D'Souza, A.A. & Devarajan, P.V. (2015) Asialoglycoprotein receptor mediated hepatocyte targeting - strategies and applications. Journal of Controlled Release, 203, 126-139. Available from: https://doi.org/10.1016/j.jconrel.2015.02.022
Dulberger, C.L., Rubin, E.J. & Boutte, C.C. (2020) The mycobacterial cell envelope - a moving target. Nature Reviews Microbiology, 18(1), 47-59. Available from: https://doi.org/10.1038/s41579-019-0273-7
Egan, A.J.F., Errington, J. & Vollmer, W. (2020) Regulation of peptidoglycan synthesis and remodelling. Nature Reviews Microbiology, 18(8), 446-460. Available from: https://doi.org/10.1038/s41579-020-0366-3
Eriksson, M., Johannssen, T., von Smolinski, D., Gruber, A., Seeberger, P. & Lepenies, B. (2013) The C-type lectin receptor SIGNR3 binds to fungi present in commensal microbiota and influences immune regulation in experimental colitis. Frontiers in Immunology, 4, 196. Available from: https://doi.org/10.3389/fimmu.2013.00196
Erwig, L.P. & Gow, N.A.R. (2016) Interactions of fungal pathogens with phagocytes. Nat Rev Micro, 14(3), 163-176. Available from: https://doi.org/10.1038/nrmicro.2015.21
Fabian, B.T., Lepenies, B., Schares, G., Dubey, J.P., Spano, F. & Seeber, F. (2021) Expanding the known repertoire of C-type lectin receptors binding to Toxoplasma gondii oocysts using a modified high-resolution immunofluorescence assay. mSphere, 6(2), e01341-20.
Faro-Trindade, I., Willment, J.A., Kerrigan, A.M., Redelinghuys, P., Hadebe, S., Reid, D.M. et al. (2012) Characterisation of innate fungal recognition in the lung. PLoS One, 7(4), e35675. Available from: https://doi.org/10.1371/journal.pone.0035675
Feinberg, H., Jégouzo, S.A.F., Lasanajak, Y., Smith, D.F., Drickamer, K., Weis, W.I. et al. (2021) Structural analysis of carbohydrate binding by the macrophage mannose receptor CD206. Journal of Biological Chemistry, 296, 100368.
Feinberg, H., Jégouzo, S.A.F., Rex, M.J., Drickamer, K., Weis, W.I. & Taylor, M.E. (2017) Mechanism of pathogen recognition by human Dectin-2. The Journal of Biological Chemistry, 292(32), 13402-13414. Available from: https://doi.org/10.1074/jbc.M117.799080
Flanagan, M.L., Arias, R.S., Hu, P., Khawli, L.A. & Epstein, A.L. (2007) Soluble Fc fusion proteins for biomedical research. Methods in Molecular Biology, 378, 33-52.
Florentin, J., Aouar, B., Dental, C., Thumann, C., Firaguay, G., Gondois-Rey, F. et al. (2012) HCV glycoprotein E2 is a novel BDCA-2 ligand and acts as an inhibitor of IFN production by plasmacytoid dendritic cells. Blood, 120(23), 4544-4551. Available from: https://doi.org/10.1182/blood-2012-02-413286
Foster, A.J., Bird, J.H., Timmer, M.S.M. & Stocker, B.L. (2016) The ligands of C-type lectins. In: Yamasaki, S. (Ed.) C-type lectin receptors in immunity. Springer Japan, pp. 191-215.
Frirdich, E., Biboy, J., Pryjma, M., Lee, J., Huynh, S., Parker, C.T. et al. (2019) The Campylobacter jejuni helical to coccoid transition involves changes to peptidoglycan and the ability to elicit an immune response. Molecular Microbiology, 112(1), 280-301.
Furukawa, A., Kamishikiryo, J., Mori, D., Toyonaga, K., Okabe, Y., Toji, A. et al. (2013) Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL. Proceedings of the National Academy of Sciences of the United States of America, 110(43), 17438-17443. Available from: https://doi.org/10.1073/pnas.1312649110
Galustian, C., Park, C.G., Chai, W., Kiso, M., Bruening, S.A., Kang, Y.S. et al. (2004) High and low affinity carbohydrate ligands revealed for murine SIGN-R1 by carbohydrate array and cell binding approaches, and differing specificities for SIGN-R3 and langerin. International Immunology, 16(6), 853-866. Available from: https://doi.org/10.1093/intimm/dxh089
Gao, S., Wake, H., Sakaguchi, M., Wang, D., Takahashi, Y., Teshigawara, K., Zhong, H., Mori, S., Liu, K., Takahashi, H. & Nishibori, M. (2020) Histidine-rich glycoprotein inhibits high-mobility group box-1-mediated pathways in vascular endothelial cells through CLEC-1A. iScience, 23(6), 101180.
Garcia-Rubio, R., de Oliveira, H.C., Rivera, J. & Trevijano-Contador, N. (2020) The fungal cell wall: candida, cryptococcus, and aspergillus species. Frontiers in Microbiology, 10, 2993. Available from: https://doi.org/10.3389/fmicb.2019.02993
Geijtenbeek, T.B.H., van Vliet, S.J., Koppel, E.A., Sanchez-Hernandez, M., Vandenbroucke-Grauls, C.M.J.E., Appelmelk, B. et al. (2003) Mycobacteria target DC-SIGN to suppress dendritic cell function. Journal of Experimental Medicine, 197(1), 7-17. Available from: https://doi.org/10.1084/jem.20021229
Geissner, A., Reinhardt, A., Rademacher, C., Johannssen, T., Monteiro, J., Lepenies, B. et al. (2019) Microbe-focused glycan array screening platform. Proceedings of the National Academy of Sciences of the United States of America, 116(6), 1958-1967. Available from: https://doi.org/10.1073/pnas.1800853116
Gomes, P.S., Feijó, D.F., Morrot, A. & Freire-de-Lima, C.G. (2017) Decoding the role of glycans in malaria. Frontiers in Microbiology, 8, 1071. Available from: https://doi.org/10.3389/fmicb.2017.01071
Goncalves, A.-R., Moraz, M.-L., Pasquato, A., Helenius, A., Lozach, P.-Y. & Kunz, S. (2013) Role of DC-SIGN in lassa virus entry into human dendritic cells. Journal of Virology, 87(21), 11504-11515. Available from: https://doi.org/10.1128/JVI.01893-13
Goyal, S., Castrillón-Betancur, J.C., Klaile, E. & Slevogt, H. (2018) The interaction of human pathogenic fungi with C-type lectin receptors. Frontiers in Immunology, 9, 1261. Available from: https://doi.org/10.3389/fimmu.2018.01261
Graham, L.M., Gupta, V., Schafer, G., Reid, D.M., Kimberg, M., Dennehy, K.M. et al. (2012) The C-type lectin receptor CLECSF8 (CLEC4D) is expressed by myeloid cells and triggers cellular activation through Syk kinase. Journal of Biological Chemistry, 287(31), 25964-25974.
Graham, L.M., Tsoni, S.V., Willment, J.A., Williams, D.L., Taylor, P.R., Gordon, S. et al. (2006) Soluble Dectin-1 as a tool to detect beta-glucans. Journal of Immunological Methods, 314(1-2), 164-169.
Graus, M.S., Wester, M.J., Lowman, D.W., Williams, D.L., Kruppa, M.D., Martinez, C.M. et al. (2018) Mannan molecular substructures control nanoscale glucan exposure in candida. Cell Reports, 24(9), 2432-2442.e5.
Gravelat, F.N., Beauvais, A., Liu, H., Lee, M.J., Snarr, B.D., Chen, D. et al. (2013) Aspergillus galactosaminogalactan mediates adherence to host constituents and conceals hyphal β-glucan from the immune system. PLoS Pathogens, 9(8), e1003575. Available from: https://doi.org/10.1371/journal.ppat.1003575
Griffith, Q., Liang, Y., Whitworth, P., Rodriguez-Russo, C., Gul, A., Siddiqui, A.A. et al. (2015) Immuno-evasive tactics by schistosomes identify an effective allergy preventative. Experimental Parasitology, 153, 139-150. Available from: https://doi.org/10.1016/j.exppara.2015.03.012
Guan, Y., Ranoa, D.R.E., Jiang, S., Mutha, S.K., Li, X., Baudry, J. et al. (2010) Human TLRs 10 and 1 share common mechanisms of innate immune sensing but not signaling. The Journal of Immunology, 184(9), 5094-5103. Available from: https://doi.org/10.4049/jimmunol.0901888
Guo, Y., Chang, Q., Cheng, L., Xiong, S., Jia, X., Lin, X. et al. (2018) C-Type lectin receptor CD23 is required for host defense against Candida albicans and Aspergillus fumigatus infection. The Journal of Immunology, 201(8), 2427-2440.
Guo, Y., Feinberg, H., Conroy, E., Mitchell, D.A., Alvarez, R., Blixt, O. et al. (2004) Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR. Nature Structural and Molecular Biology, 11(7), 591-598. Available from: https://doi.org/10.1038/nsmb784
Haryadi, R., Ho, S., Kok, Y.J., Pu, H.X., Zheng, L., Pereira, N.A. et al. (2015) Optimization of heavy chain and light chain signal peptides for high level expression of therapeutic antibodies in CHO cells. PLoS One, 10(2), e0116878. Available from: https://doi.org/10.1371/journal.pone.0116878
Heyl, K.A., Klassert, T.E., Heinrich, A., Müller, M.M., Klaile, E., Dienemann, H. et al. (2014) Dectin-1 is expressed in human lung and mediates the proinflammatory immune response to nontypeable haemophilus influenzae. MBio, 5(5), e01492-14. Available from: https://doi.org/10.1128/mBio.01492-14
Hirabayashi, J. & Arai, R. (2019) Lectin engineering: the possible and the actual. Interface Focus, 9(2), 20180068. Available from: https://doi.org/10.1098/rsfs.2018.0068
Horta, M.F., Andrade, L.O., Martins-Duarte, É.S. & Castro-Gomes, T. (2020) Cell invasion by intracellular parasites - the many roads to infection. Journal of Cell Science, 133(4), jcs232488. Available from: https://doi.org/10.1242/jcs.232488
Hsu, T.L., Cheng, S.C., Yang, W.B., Chin, S.W., Chen, B.H., Huang, M.T. et al. (2009) Profiling carbohydrate-receptor interaction with recombinant innate immunity receptor-Fc fusion proteins. Journal of Biological Chemistry, 284(50), 34479-34489. Available from: https://doi.org/10.1074/jbc.M109.065961
Huang, H.-R., Li, F., Han, H., Lv, Q.-Z., Xu, X., Li, N. et al. (2018) Dectin-3 recognizes cryptococcal glucuronoxylomannan to initiate host defense against cryptococcosis. bioRxiv, 281790.
Iborra, S., Martínez-López, M., Cueto, F.J., Conde-Garrosa, R., Del Fresno, C., Izquierdo, H.M. et al. (2016) Leishmania uses mincle to target an inhibitory ITAM signaling pathway in dendritic cells that dampens adaptive immunity to infection. Immunity, 45(4), 788-801. Available from: https://doi.org/10.1016/j.immuni.2016.09.012
Iborra, S. & Sancho, D. (2015) Signalling versatility following self and non-self sensing by myeloid C-type lectin receptors. Immunobiology, 220(2), 175-184. Available from: https://doi.org/10.1016/j.imbio.2014.09.013
Inoue, M. & Shinohara, M.L. (2014) Clustering of pattern recognition receptors for fungal detection. PLoS Pathogens, 10(2), e1003873. Available from: https://doi.org/10.1371/journal.ppat.1003873
Ishikawa, E., Ishikawa, T., Morita, Y.S., Toyonaga, K., Yamada, H., Takeuchi, O. et al. (2009) Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle. Journal of Experimental Medicine, 206(13), 2879-2888. Available from: https://doi.org/10.1084/jem.20091750
Ishikawa, T., Itoh, F., Yoshida, S., Saijo, S., Matsuzawa, T., Gonoi, T. et al. (2013) Identification of distinct ligands for the C-type lectin receptors Mincle and Dectin-2 in the pathogenic fungus Malassezia. Cell Host and Microbe, 13(4), 477-488. Availble from: https://doi.org/10.1016/j.chom.2013.03.008
Jégouzo, S.A., Feinberg, H., Dungarwalla, T., Drickamer, K., Weis, W.I. & Taylor, M.E. (2015) A novel mechanism for binding of galactose-terminated glycans by the C-type carbohydrate recognition domain in blood dendritic cell antigen 2. Journal of Biological Chemistry, 290(27), 16759-16771. Available from: https://doi.org/10.1074/jbc.M115.660613
Jégouzo, S.A.F., Feinberg, H., Morrison, A.G., Holder, A., May, A., Huang, Z. et al. (2019) CD23 is a glycan-binding receptor in some mammalian species. The Journal of Biological Chemistry, 294(41), 14845-14859. Available from: https://doi.org/10.1074/jbc.RA119.010572
Jouault, T., El Abed-El Behi, M., Martinez-Esparza, M., Breuilh, L., Trinel, P.A., Chamaillard, M. et al. (2006) Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling. Journal of Immunology, 177(7), 4679-4687.
Kerscher, B., Willment, J.A. & Brown, G.D. (2013) The Dectin-2 family of C-type lectin-like receptors: an update. International Immunology, 25(5), 271-277. Available from: https://doi.org/10.1093/intimm/dxt006
Khoo, U.-S., Chan, K.Y.K., Chan, V.S.F. & Lin, C.L.S. (2008) DC-SIGN and L-SIGN: the SIGNs for infection. Journal of Molecular Medicine, 86(8), 861-874. Available from: https://doi.org/10.1007/s00109-008-0350-2
Kottom, T.J., Hebrink, D.M., Jenson, P.E., Nandakumar, V., Wüthrich, M., Wang, H. et al. (2017) The interaction of Pneumocystis with the C-type lectin receptor Mincle exerts a significant role in host defense against infection. The Journal of Immunology, 198(9), 3515-3525.
Kottom, T.J., Hebrink, D.M., Monteiro, J.T., Lepenies, B., Carmona, E.M., Wuethrich, M. et al. (2019) Myeloid C-type lectin receptors that recognize fungal mannans interact with Pneumocystis organisms and major surface glycoprotein. Journal of Medical Microbiology, 68(11), 1649-1654. Available from: https://doi.org/10.1099/jmm.0.001062
Kumari, S., Achazi, K., Dey, P., Haag, R. & Dernedde, J. (2019) Design and synthesis of PEG-oligoglycerol sulfates as multivalent inhibitors for the scavenger receptor LOX-1. Biomacromolecules, 20(3), 1157-1166. Available from: https://doi.org/10.1021/acs.biomac.8b01416
Lambert, A.A., Gilbert, C., Richard, M., Beaulieu, A.D. & Tremblay, M.J. (2008) The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans- and cis-infection pathways. Blood, 112(4), 1299-1307. Available from: https://doi.org/10.1182/blood-2008-01-136473
Latgé, J.-P. & Chamilos, G. (2019) Aspergillus fumigatus and Aspergillosis in 2019. Clinical Microbiology Reviews, 33(1), e00140-18. Available from: https://doi.org/10.1128/CMR.00140-18
Lee, R.T., Hsu, T.-L., Huang, S.K., Hsieh, S.-L., Wong, C.-H. & Lee, Y.C. (2011) Survey of immune-related, mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities. Glycobiology, 21(4), 512-520. Available from: https://doi.org/10.1093/glycob/cwq193
Lefèvre, L., Lugo-Villarino, G., Meunier, E., Valentin, A., Olagnier, D., Authier, H. et al. (2013) The C-type lectin receptors Dectin-1, MR, and SIGNR3 contribute both positively and negatively to the macrophage response to Leishmania infantum. Immunity, 38(5), 1038-1049. Available from: https://doi.org/10.1016/j.immuni.2013.04.010
Lenardon, M.D., Sood, P., Dorfmueller, H.C., Brown, A.J.P. & Gow, N.A.R. (2020) Scalar nanostructure of the Candida albicans cell wall; a molecular, cellular and ultrastructural analysis and interpretation. The Cell Surface, 6, 100047. Available from: https://doi.org/10.1016/j.tcsw.2020.100047
Li, R.-J.-E., Hogervorst, T.P., Achilli, S., Bruijns, S.C.M., Spiekstra, S., Vivès, C. et al. (2020) Targeting of the C-Type lectin receptor langerin using bifunctional mannosylated antigens. Frontiers in Cell and Developmental Biology, 8, 556. Available from: https://doi.org/10.3389/fcell.2020.00556
Li, Z. & Feizi, T. (2018) The neoglycolipid (NGL) technology-based microarrays and future prospects. FEBS Letters, 592(23), 3976-3991.
Liedke, S.C., Miranda, D.Z., Gomes, K.X., Gonçalves, J.L.S., Frases, S., Nosanchuk, J.D. et al. (2017) Characterization of the antifungal functions of a WGA-Fc (IgG2a) fusion protein binding to cell wall chitin oligomers. Scientific Reports, 7(1), 12187. Available from: https://doi.org/10.1038/s41598-017-12540-y
Lightfoot, Y.L., Selle, K., Yang, T., Goh, Y.J., Sahay, B., Zadeh, M. et al. (2015) SIGNR3-dependent immune regulation by Lactobacillus acidophilus surface layer protein A in colitis. The EMBO Journal, 34, 881-895. Available from: https://doi.org/10.15252/embj.201490296
Linehan, S., Coulson, P., Wilson, R., Mountford, A.P., Brombacher, F., Martínez-Pomares, L. et al. (2003) IL-4 receptor signaling is required for mannose receptor expression by macrophages recruited to granulomata but not resident cells in mice infected with Schistosoma mansoni. Laboratory Investigation, 83, 1223-1231. Available from: https://doi.org/10.1097/01.LAB.0000081392.93701.6F
Lozach, P.-Y., Kühbacher, A., Meier, R., Mancini, R., Bitto, D., Bouloy, M. et al. (2011) DC-SIGN as a receptor for phleboviruses. Cell Host and Microbe, 10(1), 75-88. Available from: https://doi.org/10.1016/j.chom.2011.06.007
Maalej, M., Forgione, R.E., Marchetti, R., Bulteau, F., Thépaut, M., Lanzetta, R. et al. (2019) Human macrophage galactose-type lectin (MGL) recognizes the outer core of Escherichia coli lipooligosaccharide. ChemBioChem, 20, 1778.
Maglinao, M., Eriksson, M., Schlegel, M.K., Zimmermann, S., Johannssen, T., Götze, S. et al. (2014) A platform to screen for C-type lectin receptor-binding carbohydrates and their potential for cell-specific targeting and immune modulation. Journal of Controlled Release, 175, 36-42. Available from: https://doi.org/10.1016/j.jconrel.2013.12.011
Manabe, Y., Marchetti, R., Takakura, Y., Nagasaki, M., Nihei, W., Takebe, T. et al. (2019) The core fucose on an IgG antibody is an endogenous ligand of Dectin-1. Angewandte Chemie International Edition, 58(51), 18697-18702. Available from: https://doi.org/10.1002/anie.201911875
Marakalala, M.J., Vautier, S., Potrykus, J., Walker, L.A., Shepardson, K.M., Hopke, A. et al. (2013) Differential adaptation of Candida albicans in vivo modulates immune recognition by Dectin-1. PLoS Pathogens, 9(4), e1003315.
Marcelo, F., Supekar, N., Corzana, F., van der Horst, J.C., Vuist, I.M., Live, D. et al. (2019) Identification of a secondary binding site in human macrophage galactose-type lectin by microarray studies: implications for the molecular recognition of its ligands. Journal of Biological Chemistry, 294(4), 1300-1311. Available from: https://doi.org/10.1074/jbc.RA118.004957
Martinez-Pomares, L. (2012) The mannose receptor. Journal of Leukocyte Biology, 92(6), 1177-1186. Available from: https://doi.org/10.1189/jlb.0512231
Mattila, P.E., Metz, A.E., Rapaka, R.R., Bauer, L.D. & Steele, C. (2008) Dectin-1 Fc targeting of Aspergillus fumigatus beta-glucans augments innate defense against invasive pulmonary aspergillosis. Antimicrobial Agents and Chemotherapy, 52(3), 1171-1172.
Mayer, S., Moeller, R., Monteiro, J.T., Ellrott, K., Josenhans, C. & Lepenies, B. (2018) C-type lectin receptor (CLR)-Fc fusion proteins as tools to screen for novel CLR/bacteria interactions: an exemplary study on preselected campylobacter jejuni isolates. Frontiers in Immunology, 9, 213. Available from: https://doi.org/10.3389/fimmu.2018.00213
McGreal, E.P., Rosas, M., Brown, G.D., Zamze, S., Wong, S.Y., Gordon, S. et al. (2006) The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose. Glycobiology, 16(5), 422-430. Available from: https://doi.org/10.1093/glycob/cwj077
Mehaffy, C., Belisle, J.T. & Dobos, K.M. (2019) Mycobacteria and their sweet proteins: an overview of protein glycosylation and lipoglycosylation in M. tuberculosis. Tuberculosis (Edinb), 115, 1-13. Available from: https://doi.org/10.1016/j.tube.2019.01.001
Miller, J.L., de Wet, B.J., Martinez-Pomares, L., Radcliffe, C.M., Dwek, R.A., Rudd, P.M. et al. (2008) The mannose receptor mediates dengue virus infection of macrophages. PLoS Pathogens, 4(2), e17. Available from: https://doi.org/10.1371/journal.ppat.0040017
Mistou, M.-Y., Sutcliffe, I.C. & van Sorge, N.M. (2016) Bacterial glycobiology: rhamnose-containing cell wall polysaccharides in Gram-positive bacteria. FEMS Microbiology Reviews, 40(4), 464-479. Available from: https://doi.org/10.1093/femsre/fuw006
Mitchell, D.A., Fadden, A.J. & Drickamer, K. (2001) A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. Journal of Biological Chemistry, 276(31), 28939-28945. Available from: https://doi.org/10.1074/jbc.M104565200
Miyake, Y., Oh-hora, M. & Yamasaki, S. (2015) C-Type lectin receptor MCL facilitates mincle expression and signaling through complex formation. The Journal of Immunology. Available from: https://doi.org/10.4049/jimmunol.1402429
Miyake, Y., Toyonaga, K., Mori, D., Kakuta, S., Hoshino, Y., Oyamada, A. et al. (2013) C-type lectin MCL is an FcRγ-coupled receptor that mediates the adjuvanticity of mycobacterial cord factor. Immunity, 38(5), 1050-1062. Available from: https://doi.org/10.1016/j.immuni.2013.03.010
Mnich, M.E., van Dalen, R. & van Sorge, N.M. (2020) C-type lectin receptors in host defense against bacterial pathogens. Frontiers in Cellular and Infection Microbiology, 10, 309. Available from: https://doi.org/10.3389/fcimb.2020.00309
Modis, Y. (2014) Relating structure to evolution in class II viral membrane fusion proteins. Current Opinion in Virology, 5, 34-41. Available from: https://doi.org/10.1016/j.coviro.2014.01.009
Monteiro, J.T., Schön, K., Ebbecke, T., Goethe, R., Ruland, J., Baumgärtner, W. et al. (2019) The CARD9-associated C-type lectin, mincle, recognizes la crosse virus (LACV) but plays a limited role in early antiviral responses against LACV. Viruses, 11(3). Available from: https://doi.org/10.3390/v11030303
Mori, D., Shibata, K. & Yamasaki, S. (2017) C-Type Lectin receptor Dectin-2 binds to an endogenous protein β-glucuronidase on dendritic cells. PLoS One, 12(1), e0169562. Available from: https://doi.org/10.1371/journal.pone.0169562
Nagae, M., Ikeda, A., Hanashima, S., Kojima, T., Matsumoto, N., Yamamoto, K. et al. (2016) Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan. FEBS Letters, 590(8), 1280-1288.
Nagae, M., Morita-Matsumoto, K., Kato, M., Kaneko, M.K., Kato, Y. & Yamaguchi, Y. (2014) A platform of C-type lectin-like receptor CLEC-2 for binding O-glycosylated podoplanin and nonglycosylated rhodocytin. Structure, 22(12), 1711-1721. Available from: https://doi.org/10.1016/j.str.2014.09.009
Nagae, M., Yamanaka, K., Hanashima, S., Ikeda, A., Morita-Matsumoto, K., Satoh, T. et al. (2013) Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2. Journal of Biological Chemistry, 288(47), 33598-33610. Available from: https://doi.org/10.1074/jbc.M113.513572
Neumann, K., Castiñeiras-Vilariño, M., Höckendorf, U., Hannesschläger, N., Lemeer, S., Kupka, D. et al. (2014) Clec12a is an inhibitory receptor for uric acid crystals that regulates inflammation in response to cell death. Immunity, 40(3), 389-399. Available from: https://doi.org/10.1016/j.immuni.2013.12.015
Ohki, I., Ishigaki, T., Oyama, T., Matsunaga, S., Xie, Q., Ohnishi-Kameyama, M. et al. (2005) Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL. Structure, 13(6), 905-917. Available from: https://doi.org/10.1016/j.str.2005.03.016
Omahdi, Z., Horikawa, Y., Nagae, M., Toyonaga, K., Imamura, A., Takato, K. et al. (2020) Structural insight into the recognition of pathogen-derived phosphoglycolipids by C-type lectin receptor DCAR. Journal of Biological Chemistry, 295(17), 5807-5817. Available from: https://doi.org/10.1074/jbc.RA120.012491
Palma, A.S., Liu, Y., Zhang, H., Zhang, Y., McCleary, B.V., Yu, G. et al. (2015) Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry. Molecular and Cellular Proteomics, 14(4), 974-988. Available from: https://doi.org/10.1074/mcp.M115.048272
Palomino-Segura, M., Perez, L., Farsakoglu, Y., Virgilio, T., Latino, I., D'Antuono, R. et al. (2019) Protection against influenza infection requires early recognition by inflammatory dendritic cells through C-type lectin receptor SIGN-R1. Nature Microbiology, 4(11), 1930-1940. Available from: https://doi.org/10.1038/s41564-019-0506-6
Patin, E.C., Orr, S.J. & Schaible, U.E. (2017) Macrophage inducible C-type lectin as a multifunctional player in immunity. Frontiers in Immunology, 8, 861. Available from: https://doi.org/10.3389/fimmu.2017.00861
Patin, E.C., Thompson, A. & Orr, S.J. (2019) Pattern recognition receptors in fungal immunity. Seminars in Cell & Developmental Biology, 89, 24-33. Available from: https://doi.org/10.1016/j.semcdb.2018.03.003
Polando, R.E., Jones, B.C., Ricardo, C., Whitcomb, J., Ballhorn, W. & McDowell, M.A. (2018) Mannose receptor (MR) and Toll-like receptor 2 (TLR2) influence phagosome maturation during Leishmania infection. Parasite Immunology, 40(4), e12521.
Pradhan, A., Avelar, G.M., Bain, J.M., Childers, D., Pelletier, C., Larcombe, D.E. et al. (2019) Non-canonical signalling mediates changes in fungal cell wall PAMPs that drive immune evasion. Nature Communications, 10(1), 5315. Available from: https://doi.org/10.1038/s41467-019-13298-9
Rabes, A., Zimmermann, S., Reppe, K., Lang, R., Seeberger, P.H., Suttorp, N. et al. (2015) The C-type lectin receptor Mincle binds to Streptococcus pneumoniae but plays a limited role in the anti-pneumococcal innate immune response. PLoS One, 10(2), e0117022. Available from: https://doi.org/10.1371/journal.pone.0117022
Rapaka, R.R., Goetzman, E.S., Zheng, M., Vockley, J., McKinley, L., Kolls, J.K. et al. (2007) Enhanced defense against Pneumocystis carinii mediated by a novel Dectin-1 receptor Fc fusion protein. Journal of Immunology, 178(6), 3702-3712.
Rappleye, C.A., Eissenberg, L.G. & Goldman, W.E. (2007) Histoplasma capsulatum alpha-(1,3)-glucan blocks innate immune recognition by the beta-glucan receptor. Proceedings of the National Academy of Sciences of the United States of America, 104(4), 1366-1370.
Raulf, M.-K., Johannssen, T., Matthiesen, S., Neumann, K., Hachenberg, S., Mayer-Lambertz, S. et al. (2019) The C-type lectin receptor CLEC12A recognizes plasmodial hemozoin and contributes to cerebral malaria development. Cell Reports, 28(1), 30-38.e35. Available from: https://doi.org/10.1016/j.celrep.2019.06.015
Rayes, J., Watson, S.P. & Nieswandt, B. (2019) Functional significance of the platelet immune receptors GPVI and CLEC-2. Journal of Clinical Investigation, 129(1), 12-23. Available from: https://doi.org/10.1172/JCI122955
Redelinghuys, P., Whitehead, L., Augello, A., Drummond, R.A., Levesque, J.M., Vautier, S. et al. (2016) MICL controls inflammation in rheumatoid arthritis. Annals of the Rheumatic Diseases, 75(7), 1386-1391.
Rillahan, C.D. & Paulson, J.C. (2011) Glycan microarrays for decoding the glycome. Annual Review of Biochemistry, 80(1), 797-823. Available from: https://doi.org/10.1146/annurev-biochem-061809-152236
Rodrigues, E., Jung, J., Park, H., Loo, C., Soukhtehzari, S., Kitova, E.N. et al. (2020) A versatile soluble siglec scaffold for sensitive and quantitative detection of glycan ligands. Nature Communications, 11(1), 5091. Available from: https://doi.org/10.1038/s41467-020-18907-6
Rodriguez-de la Noval, C., Ruiz Mendoza, S., de Souza Gonçalves, D., da Silva Ferreira, M., Honorato, L., Peralta, J.M. et al. (2020) Protective efficacy of lectin-Fc(IgG) fusion proteins in vitro and in a pulmonary aspergillosis in vivo model. Journal of Fungi, 6(4), 250. Available from: https://doi.org/10.3390/jof6040250
Rothfuchs, A.G., Bafica, A., Feng, C.G., Egen, J.G., Williams, D.L., Brown, G.D. et al. (2007) Dectin-1 interaction with Mycobacterium tuberculosis leads to enhanced IL-12p40 production by splenic dendritic cells. Journal of Immunology, 179(6), 3463-3471.
Saijo, S., Ikeda, S., Yamabe, K., Kakuta, S., Ishigame, H., Akitsu, A. et al. (2010) Dectin-2 recognition of alpha-mannans and induction of Th17 cell differentiation is essential for host defense against Candida albicans. Immunity, 32(5), 681-691.
Sato, K., Yang, X.-L., Yudate, T., Chung, J.-S., Wu, J., Luby-Phelps, K. et al. (2006) Dectin-2 is a pattern recognition receptor for fungi that couples with the fc receptor γ chain to induce innate immune responses. Journal of Biological Chemistry, 281(50), 38854-38866. Available from: https://doi.org/10.1074/jbc.M606542200
Schoenen, H., Bodendorfer, B., Hitchens, K., Manzanero, S., Werninghaus, K., Nimmerjahn, F. et al. (2010) Cutting edge: Mincle is essential for recognition and adjuvanticity of the mycobacterial cord factor and its synthetic analog trehalose-dibehenate. The Journal of Immunology, 184(6), 2756-2760. Available from: https://doi.org/10.4049/jimmunol.0904013
Schulz, O., Hanc, P., Bottcher, J.P., Hoogeboom, R., Diebold, S.S., Tolar, P. et al. (2018) Myosin II synergizes with F-actin to promote DNGR-1-dependent cross-presentation of dead cell-associated antigens. Cell Reports, 24(2), 419-428. Available from: https://doi.org/10.1016/j.celrep.2018.06.038
Seiler, B., Cartwright, M., Dinis, A., Duffy, S., Lombardo, P., Cartwright, D., Super, E., Lanzaro, J., Dugas, K., Super, M. & Ingber, D. (2019). Broad-spectrum capture of clinical pathogens using engineered Fc-mannose-binding lectin enhanced by antibiotic treatment. F1000Research, 8, 108. Available from: https://doi.org/10.12688/f1000research.17447.1
Sheeley, D.M., Merrill, B.M. & Taylor, L.C. (1997) Characterization of monoclonal antibody glycosylation: comparison of expression systems and identification of terminal alpha-linked galactose. Analytical Biochemistry, 247(1), 102-110.
Shimaoka, T., Kume, N., Minami, M., Hayashida, K., Sawamura, T., Kita, T. et al. (2001) LOX-1 supports adhesion of Gram-positive and Gram-negative bacteria. Journal of Immunology, 166(8), 5108-5114.
Silva-Martín, N., Bartual, S.G., Ramírez-Aportela, E., Chacón, P., Park, C.G. & Hermoso, J.A. (2014) Structural basis for selective recognition of endogenous and microbial polysaccharides by macrophage receptor SIGN-R1. Structure, 22(11), 1595-1606.
Singh, S., Almuhanna, Y., Alshahrani, M.Y., Lowman, D., Rice, P.J., Gell, C. et al. (2020). Pseudomonas aeruginosa biofilms display carbohydrate ligands for CD206 and CD209 that interfere with their receptor function. bioRxiv, 2020.2004.2020.051292.
Singh, S.K., Streng-Ouwehand, I., Litjens, M., Weelij, D.R., García-Vallejo, J.J., van Vliet, S.J. et al. (2009) Characterization of murine MGL1 and MGL2 C-type lectins: distinct glycan specificities and tumor binding properties. Molecular Immunology, 46(6), 1240-1249.
Snyder, G.A., Ford, J., Torabi-Parizi, P., Arthos, J.A., Schuck, P., Colonna, M. et al. (2005) Characterization of DC-SIGN/R interaction with human immunodeficiency virus type 1 gp120 and ICAM molecules favors the receptor's role as an antigen-capturing rather than an adhesion receptor. Journal of Virology, 79(8), 4589-4598.
Stappers, M.H.T., Clark, A.E., Aimanianda, V., Bidula, S., Reid, D.M., Asamaphan, P. et al. (2018) Recognition of DHN-melanin by a C-type lectin receptor is required for immunity to Aspergillus. Nature, 555(7696), 382-386.
Steele, C., Rapaka, R.R., Metz, A., Pop, S.M., Williams, D.L., Gordon, S. et al. (2005) The beta-glucan receptor Dectin-1 recognizes specific morphologies of Aspergillus fumigatus. PLoS Pathogens, 1(4), e42. Available from: https://doi.org/10.1371/journal.ppat.0010042
Strand, J., Huang, C.T. & Xu, J. (2013) Characterization of Fc-fusion protein aggregates derived from extracellular domain disulfide bond rearrangements. Journal of Pharmaceutical Sciences, 102(2), 441-453. Available from: https://doi.org/10.1002/jps.23421
Strohl, W.R. (2009) Optimization of Fc-mediated effector functions of monoclonal antibodies. Current Opinion in Biotechnology, 20(6), 685-691. Available from: https://doi.org/10.1016/j.copbio.2009.10.011
Su, S.V., Hong, P., Baik, S., Negrete, O.A., Gurney, K.B. & Lee, B. (2004) DC-SIGN binds to HIV-1 glycoprotein 120 in a distinct but overlapping fashion compared with ICAM-2 and ICAM-3. Journal of Biological Chemistry, 279(18), 19122-19132. Available from: https://doi.org/10.1074/jbc.M400184200
Sung, P.-S., Chang, W.-C. & Hsieh, S.-L. (2020) CLEC5A: a promiscuous pattern recognition receptor to microbes and beyond. Advances in Experimental Medicine and Biology, 1204, 57-73.
Sung, P.-S., Huang, T.-F. & Hsieh, S.-L. (2019) Extracellular vesicles from CLEC2-activated platelets enhance dengue virus-induced lethality via CLEC5A/TLR2. Nature Communications, 10(1), 2402. Available from: https://doi.org/10.1038/s41467-019-10360-4
Sutton, B.J. & Davies, A.M. (2015) Structure and dynamics of IgE-receptor interactions: FcεRI and CD23/FcεRII. Immunological Reviews, 268(1), 222-235. Available from: https://doi.org/10.1111/imr.12340
Suzuki-Inoue, K., Inoue, O. & Ozaki, Y. (2011) Novel platelet activation receptor CLEC-2: from discovery to prospects. Journal of Thrombosis and Haemostasis, 9(Suppl 1), 44-55. Available from: https://doi.org/10.1111/j.1538-7836.2011.04335.x
Takahara, K., Arita, T., Tokieda, S., Shibata, N., Okawa, Y., Tateno, H. et al. (2012) Difference in fine specificity to polysaccharides of Candida albicans mannoprotein between mouse SIGNR1 and human DC-SIGN. Infection and Immunity, 80(5), 1699-1706. Available from: https://doi.org/10.1128/IAI.06308-11
Takahara, K., Yashima, Y., Omatsu, Y., Yoshida, H., Kimura, Y., Kang, Y.S. et al. (2004) Functional comparison of the mouse DC-SIGN, SIGNR1, SIGNR3 and Langerin, C-type lectins. International Immunology, 16(6), 819-829.
Takeuchi, O. & Akira, S. (2010) Pattern recognition receptors and inflammation. Cell, 140(6), 805-820.
Tanno, D., Yokoyama, R., Kawamura, K., Kitai, Y., Yuan, X., Ishii, K. et al. (2019) Dectin-2-mediated signaling triggered by the cell wall polysaccharides of Cryptococcus neoformans. Microbiology and Immunology, 63(12), 500-512.
Tateno, H., Mori, A., Uchiyama, N., Yabe, R., Iwaki, J., Shikanai, T. et al. (2008) Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins. Glycobiology, 18(10), 789-798.
Tateno, H., Ohnishi, K., Yabe, R., Hayatsu, N., Sato, T., Takeya, M. et al. (2010) Dual specificity of langerin to sulfated and mannosylated glycans via a single C-type carbohydrate recognition domain. Journal of Biological Chemistry, 285(9), 6390-6400.
Taylor, P.R., Brown, G.D., Herre, J., Williams, D.L., Willment, J.A., Gordon, S. (2004) The role of SIGNR1 and the beta-glucan receptor (dectin-1) in the nonopsonic recognition of yeast by specific macrophages. Journal of Immunology, 172(2), 1157-1162.
Taylor, M.E. & Drickamer, K. (2019) Mammalian sugar-binding receptors: known functions and unexplored roles. The FEBS Journal, 286(10), 1800-1814. Available from: https://doi.org/10.1111/febs.14759
Taylor, P.R., Gordon, S. & Martinez-Pomares, L. (2005) The mannose receptor: linking homeostasis and immunity through sugar recognition. Trends in Immunology, 26(2), 104-110. Available from: https://doi.org/10.1016/j.it.2004.12.001
Temming, A.R., Dekkers, G., van de Bovenkamp, F.S., Plomp, H.R., Bentlage, A.E.H., Szittner, Z. et al. (2019) Human DC-SIGN and CD23 do not interact with human IgG. Scientific Reports, 9(1), 9995. Available from: https://doi.org/10.1038/s41598-019-46484-2
Teng, O., Chen, S.T., Hsu, T.L., Sia, S.F., Cole, S., Valkenburg, S.A. et al. (2016) CLEC5A-mediated enhancement of the inflammatory response in myeloid cells contributes to influenza virus pathogenicity in vivo. Journal of Virology, 91(1), e01813-16. Available from: https://doi.org/10.1128/JVI.01813-16
Thépaut, M., Luczkowiak, J., Vivès, C., Labiod, N., Bally, I., Lasala, F., Grimoire, Y., Fenel, D., Sattin, S., Thielens, N., Schoehn, G., Bernardi, A., Delgado, R. & Fieschi, F. (2020). DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist. PLoS Pathogens, 17(5), e1009576.
Thiagarajan, P.S., Yakubenko, V.P., Elsori, D.H., Yadav, S.P., Willard, B., Tan, C.D. et al. (2013) Vimentin is an endogenous ligand for the pattern recognition receptor Dectin-1. Cardiovascular Research, 99(3), 494-504. Available from: https://doi.org/10.1093/cvr/cvt117
Thompson, A.J., de Vries, R.P. & Paulson, J.C. (2019) Virus recognition of glycan receptors. Current Opinion in Virology, 34, 117-129. Available from: https://doi.org/10.1016/j.coviro.2019.01.004
Thompson, A., Griffiths, J.S., Walker, L., da Fonseca, D.M., Lee, K.K., Taylor, P.R. et al. (2019) Dependence on Dectin-1 varies with multiple candida species. Frontiers in Microbiology, 10, 1800. Available from: https://doi.org/10.3389/fmicb.2019.01800
Tinberg, C.E., Khare, S.D., Dou, J., Doyle, L., Nelson, J.W., Schena, A. et al. (2013) Computational design of ligand-binding proteins with high affinity and selectivity. Nature, 501(7466), 212-216.
Tone, K., Stappers, M.H.T., Willment, J.A. & Brown, G.D. (2019) C-type lectin receptors of the Dectin-1 cluster: physiological roles and involvement in disease. European Journal of Immunology, 49(12), 2127-2133. Available from: https://doi.org/10.1002/eji.201847536
Torrelles, J.B., Azad, A.K. & Schlesinger, L.S. (2006) Fine discrimination in the recognition of individual species of phosphatidyl-myo-Inositol mannosides from Mycobacterium tuberculosis by C-type lectin pattern recognition receptors. The Journal of Immunology, 177(3), 1805-1816.
Toyonaga, K., Torigoe, S., Motomura, Y., Kamichi, T., Hayashi, J.M., Morita, Y.S. et al. (2016) C-type lectin receptor DCAR recognizes mycobacterial phosphatidyl-inositol mannosides to promote a th1 response during infection. Immunity, 45(6), 1245-1257. Available from: https://doi.org/10.1016/j.immuni.2016.10.012
Toyonaga, K. & Yamasaki, S. (2020) Recognition of mycobacteria by dendritic cell immunoactivating receptor. In: Yamasaki, S. (Ed.) C-type lectins in immune homeostasis. Springer International Publishing, pp. 103-115.
Valsecchi, I., Dupres, V., Michel, J.-P., Duchateau, M., Matondo, M., Chamilos, G. et al. (2019) The puzzling construction of the conidial outer layer of Aspergillus fumigatus. Cellular Microbiology, 21(5), e12994.
van Die, I. & Cummings, R.D. (2009) Glycan gimmickry by parasitic helminths: a strategy for modulating the host immune response? Glycobiology, 20(1), 2-12. Available from: https://doi.org/10.1093/glycob/cwp140
van Die, I., van Vliet, S.J., Nyame, A.K., Cummings, R.D., Bank, C.M.C., Appelmelk, B. et al. (2003) The dendritic cell-specific C-type lectin DC-SIGN is a receptor for Schistosoma mansoni egg antigens and recognizes the glycan antigen Lewis x. Glycobiology, 13(6), 471-478. Available from: https://doi.org/10.1093/glycob/cwg052
van Liempt, E., Bank, C.M.C., Mehta, P., Garcı´a-Vallejo, J.J., Kawar, Z.S., Geyer, R. et al. (2006) Specificity of DC-SIGN for mannose- and fucose-containing glycans. FEBS Letters, 580(26), 6123-6131. Available from: https://doi.org/10.1016/j.febslet.2006.10.009
van Kooyk, Y., Ilarregui, J.M. & van Vliet, S.J. (2015) Novel insights into the immunomodulatory role of the dendritic cell and macrophage-expressed C-type lectin MGL. Immunobiology, 220(2), 185-192. Available from: https://doi.org/10.1016/j.imbio.2014.10.002
Van Sorge, N.M., Bleumink, N.M.C., Van Vliet, S.J., Saeland, E., Van Der Pol, W.-L., Van Kooyk, Y. et al. (2009) N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL. Cellular Microbiology, 11(12), 1768-1781.
van Vliet, S.J., Steeghs, L., Bruijns, S.C.M., Vaezirad, M.M., Snijders Blok, C., Arenas Busto, J.A. et al. (2009) Variation of Neisseria gonorrhoeae lipooligosaccharide directs dendritic cell-induced T helper responses. PLoS Path, 5(10), e1000625. Available from: https://doi.org/10.1371/journal.ppat.1000625
van Vliet, S.J., van Liempt, E., Saeland, E., Aarnoudse, C.A., Appelmelk, B., Irimura, T. et al. (2005) Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells. International Immunology, 17(5), 661-669. Available from: https://doi.org/10.1093/intimm/dxh246
Varki, A., Schnaar, R.L. & Schauer, R. (2015) Sialic acids and other nonulosonic acids. In: Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M. et al. (Eds.) Essentials of glycobiology. Cold Spring Harbor Laboratory Press, pp. 179-195.
Vendele, I., Willment, J.A., Silva, L.M., Palma, A.S., Chai, W., Liu, Y. et al. (2020) Mannan detecting C-type lectin receptor probes recognise immune epitopes with diverse chemical, spatial and phylogenetic heterogeneity in fungal cell walls. PLoS Pathogens, 16(1), e1007927. Available from: https://doi.org/10.1371/journal.ppat.1007927
Veríssimo, C.M., Graeff-Teixeira, C., Jones, M.K. & Morassutti, A.L. (2019) Glycans in the roles of parasitological diagnosis and host-parasite interplay. Parasitology, 146(10), 1217-1232. Available from: https://doi.org/10.1017/S0031182019000465
Viriyakosol, S., Fierer, J., Brown, G.D., Kirkland, T.N. (2005) Innate immunity to the pathogenic fungus Coccidioides posadasii is dependent on Toll-like receptor 2 and Dectin-1. Infection and Immunity, 73(3), 1553-1560.Available from: https://doi.org/10.1128/IAI.73.3.1553-1560.2005
Walsh, N.M., Wuthrich, M., Wang, H., Klein, B. & Hull, C.M. (2017) Characterization of C-type lectins reveals an unexpectedly limited interaction between Cryptococcus neoformans spores and Dectin-1. PLoS One, 12(3), e0173866. Available from: https://doi.org/10.1371/journal.pone.0173866
Wang, H., LeBert, V., Hung, C.Y., Galles, K., Saijo, S., Lin, X. et al. (2014) C-type lectin receptors differentially induce Th17 cells and vaccine immunity to the endemic mycosis of North America. The Journal of Immunology, 192(3), 1107-1119. Available from: https://www.jimmunol.org/content/192/3/1107
Watanabe, N., Kidokoro, M., Suzuki, Y., Tanaka, M., Inoue, S., Tsukamoto, H. et al. (2019) A pull-down and slot blot-based screening system for inhibitor compounds of the podoplanin-CLEC-2 interaction. PLoS One, 14(9), e0222331. Available from: https://doi.org/10.1371/journal.pone.0222331
Weidenmaier, C. & Peschel, A. (2008) Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nature Reviews Microbiology, 6(4), 276-287. Available from: https://doi.org/10.1038/nrmicro1861
Whitfield, C., Szymanski, C.M. & Aebi, M. (2015) Eubacteria. In: Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M. et al. (Eds.) Essentials of glycobiology. Cold Spring Harbor Laboratory Press, pp. 265-282.
WHO (2012) Vector-borne and parasitic diseases. Available from: https://www.euro.who.int/en/health-topics/communicable-diseases/vector-borne-and-parasitic-diseases/soil-transmitted-helminths/data-and-statistics
WHO. (2020) Tuberculosis. WHO. Available from: https://www.who.int/news-room/fact-sheets/detail/tuberculosis
Wilson, G.J., Marakalala, M.J., Hoving, J.C., van Laarhoven, A., Drummond, R.A., Kerscher, B. et al. (2015) The C-type lectin receptor CLECSF8/CLEC4D is a key component of anti-mycobacterial immunity. Cell Host and Microbe, 17(2), 252-259. Available from: https://doi.org/10.1016/j.chom.2015.01.004
Yamasaki, S., Ishikawa, E., Sakuma, M., Hara, H., Ogata, K., Saito, T. (2008) Mincle is an ITAM-coupled activating receptor that senses damaged cells. Nature Immunology, 9(10), 1179-1188. Available from: https://doi.org/10.1038/ni.1651
Yamasaki, S., Matsumoto, M., Takeuchi, O., Matsuzawa, T., Ishikawa, E., Sakuma, M. et al. (2009) C-type lectin Mincle is an activating receptor for pathogenic fungus, Malassezia. Proceedings of the National Academy of Sciences of the United States of America, 106(6), 1897-1902. Available from: https://doi.org/10.1073/pnas.0805177106
Yonekawa, A., Saijo, S., Hoshino, Y., Miyake, Y., Ishikawa, E., Suzukawa, M. et al. (2014) GBS. Immunity, 41(3), 402-413.
Zamze, S., Martinez-Pomares, L., Jones, H., Taylor, P.R., Stillion, R.J., Gordon, S. et al. (2002) Recognition of bacterial capsular polysaccharides and lipopolysaccharides by the macrophage mannose receptor. Journal of Biological Chemistry, 277(44), 41613-41623. Available from: https://doi.org/10.1074/jbc.M207057200
Zhang, H., Palma, A.S., Zhang, Y., Childs, R.A., Liu, Y., Mitchell, D.A. et al. (2016) Generation and characterization of β1,2-gluco-oligosaccharide probes from Brucella abortus cyclic β-glucan and their recognition by C-type lectins of the immune system. Glycobiology, 26(10), 1086-1096.
Zhang, L., Tian, Y., Wen, Z., Zhang, F., Qi, Y., Huang, W. et al. (2016) Asialoglycoprotein receptor facilitates infection of PLC/PRF/5 cells by HEV through interaction with ORF2. Journal of Medical Virology, 88(12), 2186-2195. Available from: https://doi.org/10.1002/jmv.24570
Zheng, R.B., Jégouzo, S.A.F., Joe, M., Bai, Y., Tran, H.-A., Shen, K. et al. (2017) Insights into interactions of mycobacteria with the host innate immune system from a novel array of synthetic mycobacterial glycans. ACS Chemical Biology, 12(12), 2990-3002. Available from: https://doi.org/10.1021/acschembio.7b00797
Zhu, L.L., Zhao, X.Q., Jiang, C., You, Y., Chen, X.P., Jiang, Y.Y. et al. (2013) C-type lectin receptors Dectin-3 and Dectin-2 form a heterodimeric pattern-recognition receptor for host defense against fungal infection. Immunity, 39(2), 324-334. Available from: https://doi.org/10.1016/j.immuni.2013.05.017
Zimara, N., Chanyalew, M., Aseffa, A., van Zandbergen, G., Lepenies, B., Schmid, M. et al. (2018) Dectin-1 positive dendritic cells expand after infection with leishmania major parasites and represent promising targets for vaccine development. Frontiers in Immunology, 9, 263. Available from: https://doi.org/10.3389/fimmu.2018.00263

Auteurs

Janet A Willment (JA)

Medical Research Council Centre for Medical Mycology, University of Exeter, Exeter, UK.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH