Architecture of the mycobacterial type VII secretion system.

Actinobacteria / chemistry Adenosine Triphosphatases / chemistry Adenosine Triphosphate / metabolism Cryoelectron Microscopy Models, Molecular Mycobacterium smegmatis / chemistry Protein Domains Protein Structure, Quaternary Protein Subunits / chemistry Structure-Activity Relationship Thermomonospora Type VII Secretion Systems / chemistry

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
12 2019
Historique:
received: 23 12 2018
accepted: 06 09 2019
pubmed: 10 10 2019
medline: 15 2 2020
entrez: 10 10 2019
Statut: ppublish

Résumé

Host infection by pathogenic mycobacteria, such as Mycobacterium tuberculosis, is facilitated by virulence factors that are secreted by type VII secretion systems

Identifiants

DOI: 10.1038/s41586-019-1633-1 PMID: 31597161 PMC: PMC6914368
pubmed: 31597161
doi: 10.1038/s41586-019-1633-1
pii: 10.1038/s41586-019-1633-1
pmc: PMC6914368
mid: EMS84940
doi:

Substances chimiques

Protein Subunits 0
Type VII Secretion Systems 0
Adenosine Triphosphate 8L70Q75FXE
Adenosine Triphosphatases EC 3.6.1.-

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

321-325

Subventions

Organisme : Medical Research Council
ID : MC_U105184326
Pays : United Kingdom

Références

Gröschel, M. I., Sayes, F., Simeone, R., Majlessi, L. & Brosch, R. ESX secretion systems: mycobacterial evolution to counter host immunity. Nat. Rev. Microbiol. 14, 677–691 (2016).
pubmed: 27665717 doi: 10.1038/nrmicro.2016.131
Costa, T. R. et al. Secretion systems in Gram-negative bacteria: structural and mechanistic insights. Nat. Rev. Microbiol. 13, 343–359 (2015).
pubmed: 25978706 doi: 10.1038/nrmicro3456
Maciąg, A., Piazza, A., Riccardi, G. & Milano, A. Transcriptional analysis of ESAT-6 cluster 3 in Mycobacterium smegmatis. BMC Microbiol. 9, 48 (2009).
pubmed: 19257911 pmcid: 2660348 doi: 10.1186/1471-2180-9-48
Rodriguez, G. M., Voskuil, M. I., Gold, B., Schoolnik, G. K. & Smith, I. ideR, an essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Infect. Immun. 70, 3371–3381 (2002).
pubmed: 12065475 pmcid: 128082 doi: 10.1128/IAI.70.7.3371-3381.2002
Siegrist, M. S. et al. Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition. Proc. Natl Acad. Sci. USA 106, 18792–18797 (2009).
pubmed: 19846780 doi: 10.1073/pnas.0900589106 pmcid: 2774023
Serafini, A., Boldrin, F., Palù, G. & Manganelli, R. Characterization of a Mycobacterium tuberculosis ESX-3 conditional mutant: essentiality and rescue by iron and zinc. J. Bacteriol. 191, 6340–6344 (2009).
pubmed: 19684129 pmcid: 2753049 doi: 10.1128/JB.00756-09
Tufariello, J. M. et al. Separable roles for Mycobacterium tuberculosis ESX-3 effectors in iron acquisition and virulence. Proc. Natl Acad. Sci. USA 113, E348–E357 (2016).
pubmed: 26729876 doi: 10.1073/pnas.1523321113 pmcid: 4725510
Tinaztepe, E. et al. Role of metal-dependent regulation of ESX-3 secretion in intracellular survival of Mycobacterium tuberculosis. Infect. Immun. 84, 2255–2263 (2016).
pubmed: 27245412 pmcid: 4962639 doi: 10.1128/IAI.00197-16
Mehra, A. et al. Mycobacterium tuberculosis type VII secreted effector EsxH targets host ESCRT to impair trafficking. PLoS Pathog. 9, e1003734 (2013).
pubmed: 24204276 pmcid: 3814348 doi: 10.1371/journal.ppat.1003734
Portal-Celhay, C. et al. Mycobacterium tuberculosis EsxH inhibits ESCRT-dependent CD4
pubmed: 27918526 pmcid: 5453184 doi: 10.1038/nmicrobiol.2016.232
Mittal, E. et al. Mycobacterium tuberculosis type VII secretion system effectors differentially impact the ESCRT endomembrane damage response. MBio 9, e01765-18 (2018).
pubmed: 30482832 pmcid: 6282207 doi: 10.1128/mBio.01765-18
Ohol, Y. M. et al. Mycobacterium tuberculosis MycP1 protease plays a dual role in regulation of ESX-1 secretion and virulence. Cell Host Microbe 7, 210–220 (2010).
pubmed: 20227664 pmcid: 3121311 doi: 10.1016/j.chom.2010.02.006
Brodin, P. et al. Dissection of ESAT-6 system 1 of Mycobacterium tuberculosis and impact on immunogenicity and virulence. Infect. Immun. 74, 88–98 (2006).
pubmed: 16368961 pmcid: 1346617 doi: 10.1128/IAI.74.1.88-98.2006
Siegrist, M. S. et al. Mycobacterial Esx-3 requires multiple components for iron acquisition. MBio 5, e01073-14 (2014).
pubmed: 24803520 pmcid: 4010830 doi: 10.1128/mBio.01073-14
Houben, E. N. et al. Composition of the type VII secretion system membrane complex. Mol. Microbiol. 86, 472–484 (2012).
pubmed: 22925462 doi: 10.1111/j.1365-2958.2012.08206.x
Abdallah, A. M. et al. A specific secretion system mediates PPE41 transport in pathogenic mycobacteria. Mol. Microbiol. 62, 667–679 (2006).
pubmed: 17076665 doi: 10.1111/j.1365-2958.2006.05409.x
van Winden, V. J. et al. Mycosins are required for the stabilization of the ESX-1 and ESX-5 type VII secretion membrane complexes. MBio 7, e01471-16 (2016).
pubmed: 27795391 pmcid: 5082899
Gray, T. A. et al. Intercellular communication and conjugation are mediated by ESX secretion systems in mycobacteria. Science 354, 347–350 (2016).
pubmed: 27846571 doi: 10.1126/science.aag0828 pmcid: 8324006
Beckham, K. S. et al. Structure of the mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis. Nat. Microbiol. 2, 17047 (2017).
pubmed: 28394313 doi: 10.1038/nmicrobiol.2017.47
Rosenberg, O. S. et al. Substrates control multimerization and activation of the multi-domain ATPase motor of type VII secretion. Cell 161, 501–512 (2015).
pubmed: 25865481 pmcid: 4409929 doi: 10.1016/j.cell.2015.03.040
Wagner, J. M. et al. Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct. Biol. 16, 5 (2016).
pubmed: 26922638 pmcid: 4769845 doi: 10.1186/s12900-016-0056-6
Solomonson, M. et al. Structure of the mycosin-1 protease from the mycobacterial ESX-1 protein type VII secretion system. J. Biol. Chem. 288, 17782–17790 (2013).
pubmed: 23620593 pmcid: 3682577 doi: 10.1074/jbc.M113.462036
Zhang, X. L. et al. Core component EccB1 of the Mycobacterium tuberculosis type VII secretion system is a periplasmic ATPase. FASEB J. 29, 4804–4814 (2015).
pubmed: 26396239 doi: 10.1096/fj.15-270843
Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63–65 (2014).
doi: 10.1038/nmeth.2727 pubmed: 24213166
McGowan, S. et al. X-ray crystal structure of the streptococcal specific phage lysin PlyC. Proc. Natl Acad. Sci. USA 109, 12752–12757 (2012).
pubmed: 22807482 doi: 10.1073/pnas.1208424109 pmcid: 3412044
Zoltner, M. et al. EssC: domain structures inform on the elusive translocation channel in the type VII secretion system. Biochem. J. 473, 1941–1952 (2016).
pubmed: 27130157 doi: 10.1042/BCJ20160257
Arbing, M. A. et al. Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. PLoS ONE 8, e81753 (2013).
pubmed: 24312350 pmcid: 3843698 doi: 10.1371/journal.pone.0081753
Rueden, C. T. et al. ImageJ2: ImageJ for the next generation of scientific image data. BMC Bioinformatics 18, 529 (2017).
pubmed: 29187165 pmcid: 5708080 doi: 10.1186/s12859-017-1934-z
Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017).
pubmed: 28250466 pmcid: 5494038 doi: 10.1038/nmeth.4193
Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016).
pubmed: 26592709 pmcid: 4711343 doi: 10.1016/j.jsb.2015.11.003
Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife 7, e42166 (2018).
pubmed: 30412051 pmcid: 6250425 doi: 10.7554/eLife.42166
Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290–296 (2017).
doi: 10.1038/nmeth.4169 pubmed: 28165473
Grant, T., Rohou, A. & Grigorieff, N. cisTEM, user-friendly software for single-particle image processing. eLife 7, e35383 (2018).
pubmed: 29513216 pmcid: 5854467 doi: 10.7554/eLife.35383
de la Rosa-Trevín, J. M. et al. Scipion: a software framework toward integration, reproducibility and validation in 3D electron microscopy. J. Struct. Biol. 195, 93–99 (2016).
pubmed: 27108186 doi: 10.1016/j.jsb.2016.04.010
Källberg, M. et al. Template-based protein structure modeling using the RaptorX web server. Nat. Protoc. 7, 1511–1522 (2012).
pubmed: 22814390 pmcid: 4730388 doi: 10.1038/nprot.2012.085
Yang, J. and Zhang, Y. Protein structure and function prediction using I-TASSER. Curr. Protoc. Bioinform. 52, 5.8.1–5.8.15 (2015).
doi: 10.1002/0471250953.bi0508s52
Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N. & Sternberg, M. J. The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10, 845–858 (2015).
pubmed: 25950237 pmcid: 5298202 doi: 10.1038/nprot.2015.053
Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
pubmed: 15264254 doi: 10.1002/jcc.20084
Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D 68, 352–367 (2012).
pubmed: 22505256 pmcid: 3322595 doi: 10.1107/S0907444912001308
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486–501 (2010).
pubmed: 20383002 pmcid: 2852313 doi: 10.1107/S0907444910007493
Zimmermann, L. et al. A completely reimplemented MPI bioinformatics toolkit with a new HHpred server at its core. J. Mol. Biol. 430, 2237–2243 (2018).
pubmed: 29258817 doi: 10.1016/j.jmb.2017.12.007
Mostosi, P., Schindelin, H., Kollmannsberger, P. & Thorn, A. Automated interpretation of cryo-EM density maps with convolutional neural networks. Preprint at https://www.biorxiv.org/content/10.1101/644476v1 (2019).
Kessner, D., Chambers, M., Burke, R., Agus, D. & Mallick, P. ProteoWizard: open source software for rapid proteomics tools development. Bioinformatics 24, 2534–2536 (2008).
pubmed: 18606607 pmcid: 2732273 doi: 10.1093/bioinformatics/btn323
Götze, M. et al. Automated assignment of MS/MS cleavable cross-links in protein 3D-structure analysis. J. Am. Soc. Mass Spectrom. 26, 83–97 (2015).
pubmed: 25261217 doi: 10.1007/s13361-014-1001-1
Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367–1372 (2008).
pubmed: 19029910 doi: 10.1038/nbt.1511
Fitzpatrick, A. W. P. et al. Structure of the MacAB–TolC ABC-type tripartite multidrug efflux pump. Nat. Microbiol. 2, 17070 (2017).
pubmed: 28504659 pmcid: 5447821 doi: 10.1038/nmicrobiol.2017.70

Auteurs

Nikolaos Famelis (N)

Institute for Molecular Infection Biology, Julius-Maximilians-University Würzburg, Würzburg, Germany.
Rudolf Virchow Center for Experimental Biomedicine, Julius-Maximilians-University Würzburg, Würzburg, Germany.

Angel Rivera-Calzada (A)

Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Madrid, Spain.

Gianluca Degliesposti (G)

MRC Laboratory of Molecular Biology, Cambridge, UK.

Maria Wingender (M)

Institute for Molecular Infection Biology, Julius-Maximilians-University Würzburg, Würzburg, Germany.
Rudolf Virchow Center for Experimental Biomedicine, Julius-Maximilians-University Würzburg, Würzburg, Germany.

Nicole Mietrach (N)

Institute for Molecular Infection Biology, Julius-Maximilians-University Würzburg, Würzburg, Germany.
Rudolf Virchow Center for Experimental Biomedicine, Julius-Maximilians-University Würzburg, Würzburg, Germany.

J Mark Skehel (JM)

MRC Laboratory of Molecular Biology, Cambridge, UK.

Rafael Fernandez-Leiro (R)

Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Madrid, Spain.

Bettina Böttcher (B)

Rudolf Virchow Center for Experimental Biomedicine, Julius-Maximilians-University Würzburg, Würzburg, Germany.
Rudolf Virchow Center for Experimental Biomedicine, Electron Microscopy Facility, Julius-Maximilians-University Würzburg, Würzburg, Germany.

Andreas Schlosser (A)

Rudolf Virchow Center for Experimental Biomedicine, Julius-Maximilians-University Würzburg, Würzburg, Germany.

Oscar Llorca (O)

Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Madrid, Spain. ollorca@cnio.es.

Sebastian Geibel (S)

Institute for Molecular Infection Biology, Julius-Maximilians-University Würzburg, Würzburg, Germany. sebastian.geibel@uni-wuerzburg.de.
Rudolf Virchow Center for Experimental Biomedicine, Julius-Maximilians-University Würzburg, Würzburg, Germany. sebastian.geibel@uni-wuerzburg.de.

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Classifications MeSH

questionsmedicales.fr › Bactéries › Bactéries à Gram positif › Bâtonnets à Gram positif › Bâtonnets asporogènes à Gram positif › Bâtonnets asporogènes irréguliers à Gram positif › Actinobacteria › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Acid anhydride hydrolases › Adenosine triphosphatases › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléotides adényliques › Adénosine triphosphate › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Techniques d'investigation › Microscopie électronique › Cryomicroscopie électronique › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Bactéries › Bactéries à Gram positif › Bâtonnets à Gram positif › Bâtonnets asporogènes à Gram positif › Bâtonnets asporogènes réguliers à Gram positif › Mycobacteriaceae › Mycobacterium › Mycobactéries non tuberculeuses › Mycobacterium smegmatis › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure quaternaire des protéines › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Sous-unités de protéines › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Relation structure-activité › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Bactéries › Bactéries à Gram positif › Bâtonnets à Gram positif › Bâtonnets asporogènes à Gram positif › Bâtonnets asporogènes irréguliers à Gram positif › Actinobacteria › Thermomonospora › Architecture of the mycobacterial type VII...
questionsmedicales.fr › Structures macromoléculaires › Complexes multiprotéiques › Systèmes de translocation des protéines › Systèmes bactériens de sécrétion › Systèmes de sécrétion de type VII › Architecture of the mycobacterial type VII...