LDLRAD3 is a receptor for Venezuelan equine encephalitis virus.
Animals
CRISPR-Cas Systems
/ genetics
Cell Line
Encephalitis Virus, Venezuelan Equine
/ metabolism
Encephalomyelitis, Venezuelan Equine
/ metabolism
Female
Genetic Complementation Test
Humans
Male
Mice
Mice, Inbred C57BL
Protein Binding
Receptors, LDL
/ deficiency
Receptors, Virus
/ genetics
Virus Attachment
Virus Internalization
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
12 2020
12 2020
Historique:
received:
27
04
2020
accepted:
30
09
2020
pubmed:
20
11
2020
medline:
2
3
2021
entrez:
19
11
2020
Statut:
ppublish
Résumé
Venezuelan equine encephalitis virus (VEEV) is a neurotropic alphavirus transmitted by mosquitoes that causes encephalitis and death in humans
Identifiants
pubmed: 33208938
doi: 10.1038/s41586-020-2915-3
pii: 10.1038/s41586-020-2915-3
pmc: PMC7769003
mid: NIHMS1634151
doi:
Substances chimiques
LDLRAD3 protein, human
0
Receptors, LDL
0
Receptors, Virus
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
308-314Subventions
Organisme : NIAID NIH HHS
ID : R01 AI095436
Pays : United States
Organisme : NIAID NIH HHS
ID : T32 AI007172
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI142759
Pays : United States
Organisme : NIAID NIH HHS
ID : HHSN272201700060C
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI153209
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI143673
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI142790
Pays : United States
Commentaires et corrections
Type : CommentIn
Références
Sharma, A. & Knollmann-Ritschel, B. Current understanding of the molecular basis of Venezuelan equine encephalitis virus pathogenesis and vaccine development. Viruses 11, 164 (2019).
doi: 10.3390/v11020164
Weaver, S. C. & Barrett, A. D. Transmission cycles, host range, evolution and emergence of arboviral disease. Nat. Rev. Microbiol. 2, 789–801 (2004).
doi: 10.1038/nrmicro1006
Aguilar, P. V. et al. Endemic Venezuelan equine encephalitis in the Americas: hidden under the dengue umbrella. Future Virol. 6, 721–740 (2011).
doi: 10.2217/fvl.11.50
Zhang, R. et al. Mxra8 is a receptor for multiple arthritogenic alphaviruses. Nature 557, 570–574 (2018).
doi: 10.1038/s41586-018-0121-3
Basore, K. et al. Cryo-EM structure of Chikungunya virus in complex with the Mxra8 receptor. Cell 177, 1725–1737.e16 (2019).
doi: 10.1016/j.cell.2019.04.006
Malygin, A. A. et al. C-terminal fragment of human laminin-binding protein contains a receptor domain for Venezuelan equine encephalitis and tick-borne encephalitis viruses. Biochemistry (Mosc) 74, 1328–1336 (2009).
doi: 10.1134/S0006297909120050
Ludwig, G. V., Kondig, J. P. & Smith, J. F. A putative receptor for Venezuelan equine encephalitis virus from mosquito cells. J. Virol. 70, 5592–5599 (1996).
doi: 10.1128/JVI.70.8.5592-5599.1996
Klimstra, W. B., Nangle, E. M., Smith, M. S., Yurochko, A. D. & Ryman, K. D. DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses. J. Virol. 77, 12022–12032 (2003).
doi: 10.1128/JVI.77.22.12022-12032.2003
Bernard, K. A., Klimstra, W. B. & Johnston, R. E. Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice. Virology 276, 93–103 (2000).
doi: 10.1006/viro.2000.0546
Yin, J., Gardner, C. L., Burke, C. W., Ryman, K. D. & Klimstra, W. B. Similarities and differences in antagonism of neuron alpha/beta interferon responses by Venezuelan equine encephalitis and Sindbis alphaviruses. J. Virol. 83, 10036–10047 (2009).
doi: 10.1128/JVI.01209-09
Ryman, K. D. et al. Heparan sulfate binding can contribute to the neurovirulence of neuroadapted and nonneuroadapted Sindbis viruses. J. Virol. 81, 3563–3573 (2007).
doi: 10.1128/JVI.02494-06
Gardner, C. L., Ebel, G. D., Ryman, K. D. & Klimstra, W. B. Heparan sulfate binding by natural eastern equine encephalitis viruses promotes neurovirulence. Proc. Natl Acad. Sci. USA 108, 16026–16031 (2011).
doi: 10.1073/pnas.1110617108
Tanaka, A. et al. Genome-wide screening uncovers the significance of N-sulfation of heparan sulfate as a host cell factor for Chikungunya virus infection. J. Virol. 91, e00432-17 (2017).
doi: 10.1128/JVI.00432-17
Li, W. et al. MAGeCK enables robust identification of essential genes from genome-scale CRISPR/Cas9 knockout screens. Genome Biol. 15, 554 (2014).
doi: 10.1186/s13059-014-0554-4
Diez-Roux, G. et al. A high-resolution anatomical atlas of the transcriptome in the mouse embryo. PLoS Biol. 9, e1000582 (2011).
doi: 10.1371/journal.pbio.1000582
Ranganathan, S. et al. LRAD3, a novel low-density lipoprotein receptor family member that modulates amyloid precursor protein trafficking. J. Neurosci. 31, 10836–10846 (2011).
doi: 10.1523/JNEUROSCI.5065-10.2011
Noyes, N. C., Hampton, B., Migliorini, M. & Strickland, D. K. Regulation of itch and Nedd4 E3 ligase activity and degradation by LRAD3. Biochemistry 55, 1204–1213 (2016).
doi: 10.1021/acs.biochem.5b01218
Smith, S. A. et al. Isolation and characterization of broad and ultrapotent human monoclonal antibodies with therapeutic activity against Chikungunya virus. Cell Host Microbe 18, 86–95 (2015).
doi: 10.1016/j.chom.2015.06.009
Ryman, K. D., Meier, K. C., Gardner, C. L., Adegboyega, P. A. & Klimstra, W. B. Non-pathogenic Sindbis virus causes hemorrhagic fever in the absence of alpha/beta and gamma interferons. Virology 368, 273–285 (2007).
doi: 10.1016/j.virol.2007.06.039
Sun, C., Gardner, C. L., Watson, A. M., Ryman, K. D. & Klimstra, W. B. Stable, high-level expression of reporter proteins from improved alphavirus expression vectors to track replication and dissemination during encephalitic and arthritogenic disease. J. Virol. 88, 2035–2046 (2014).
doi: 10.1128/JVI.02990-13
Davis, N. L., Willis, L. V., Smith, J. F. & Johnston, R. E. In vitro synthesis of infectious Venezuelan equine encephalitis virus RNA from a cDNA clone: analysis of a viable deletion mutant. Virology 171, 189–204 (1989).
doi: 10.1016/0042-6822(89)90526-6
Kinney, R. M. et al. Attenuation of Venezuelan equine encephalitis virus strain TC-83 is encoded by the 5′-noncoding region and the E2 envelope glycoprotein. J. Virol. 67, 1269–1277 (1993).
doi: 10.1128/JVI.67.3.1269-1277.1993
Anishchenko, M. et al. Generation and characterization of closely related epizootic and enzootic infectious cDNA clones for studying interferon sensitivity and emergence mechanisms of Venezuelan equine encephalitis virus. J. Virol. 78, 1–8 (2004).
doi: 10.1128/JVI.78.1.1-8.2004
Kim, A. S. et al. Protective antibodies against Eastern equine encephalitis virus bind to epitopes in domains A and B of the E2 glycoprotein. Nat. Microbiol. 4, 187–197 (2019).
doi: 10.1038/s41564-018-0286-4
Lubman, O. Y. et al. Rodent herpesvirus Peru encodes a secreted chemokine decoy receptor. J. Virol. 88, 538–546 (2014).
doi: 10.1128/JVI.02729-13
Sanjana, N. E., Shalem, O. & Zhang, F. Improved vectors and genome-wide libraries for CRISPR screening. Nat. Methods 11, 783–784 (2014).
doi: 10.1038/nmeth.3047
Willnow, T. E. et al. RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors. EMBO J. 15, 2632–2639 (1996).
doi: 10.1002/j.1460-2075.1996.tb00623.x
Ko, S. Y. et al. A virus-like particle vaccine prevents equine encephalitis virus infection in nonhuman primates. Sci. Transl. Med. 11, eaav3113 (2019).
doi: 10.1126/scitranslmed.aav3113
Pal, P. et al. Development of a highly protective combination monoclonal antibody therapy against Chikungunya virus. PLoS Pathog. 9, e1003312 (2013).
doi: 10.1371/journal.ppat.1003312