Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
19 01 2022
19 01 2022
Historique:
received:
12
09
2021
accepted:
04
01
2022
entrez:
20
1
2022
pubmed:
21
1
2022
medline:
16
2
2022
Statut:
epublish
Résumé
Bacterial type IV secretion systems (T4SSs) are largely responsible for the proliferation of multi-drug resistance. We solved the structure of the outer-membrane core complex (OMCC
Identifiants
pubmed: 35046412
doi: 10.1038/s41467-022-28058-5
pii: 10.1038/s41467-022-28058-5
pmc: PMC8770708
doi:
Substances chimiques
Escherichia coli Proteins
0
Type IV Secretion Systems
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
379Subventions
Organisme : NIAID NIH HHS
ID : R21 AI142378
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM138301
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131892
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM048746
Pays : United States
Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2022. The Author(s).
Références
Waksman, G. From conjugation to T4S systems in Gram-negative bacteria: a mechanistic biology perspective. EMBO Rep. 20, e47012 (2019).
pubmed: 30602585
pmcid: 6362355
doi: 10.15252/embr.201847012
Costa, T. R. D. et al. Type IV secretion systems: advances in structure, function, and activation. Mol. Microbiol. 115, 436–452 (2021).
pubmed: 33326642
pmcid: 8026593
doi: 10.1111/mmi.14670
Cascales, E. & Christie, P. J. The versatile bacterial type IV secretion systems. Nat. Rev. Microbiol. 1, 137–149 (2003).
pubmed: 15035043
doi: 10.1038/nrmicro753
de la Cruz, F., Frost, L. S., Meyer, R. J. & Zechner, E. L. Conjugative DNA metabolism in Gram-negative bacteria. FEMS Microbiol. Rev. 34, 18–40 (2010).
pubmed: 19919603
doi: 10.1111/j.1574-6976.2009.00195.x
Grohmann, E., Christie, P. J., Waksman, G. & Backert, S. Type IV secretion in Gram-negative and Gram-positive bacteria. Mol. Microbiol. 107, 455–471 (2018).
pubmed: 29235173
pmcid: 5796862
doi: 10.1111/mmi.13896
Alvarez-Martinez, C. E. & Christie, P. J. Biological diversity of prokaryotic type IV secretion systems. Microbiol. Mol. Biol. Rev. 73, 775–808 (2009).
pubmed: 19946141
pmcid: 2786583
doi: 10.1128/MMBR.00023-09
Low, H. H. et al. Structure of a type IV secretion system. Nature 508, 550–553 (2014).
pubmed: 24670658
pmcid: 3998870
doi: 10.1038/nature13081
Ghigo, J. M. Natural conjugative plasmids induce bacterial biofilm development. Nature 412, 442–445 (2001).
pubmed: 11473319
doi: 10.1038/35086581
Clarke, M., Maddera, L., Harris, R. L. & Silverman, P. M. F-pili dynamics by live-cell imaging. Proc. Natl. Acad. Sci. USA 105, 17978–17981 (2008).
pubmed: 19004777
pmcid: 2582581
doi: 10.1073/pnas.0806786105
Shaffer, C. L. et al. Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacteria-host cell interface. PLoS Path 7, e1002237 (2011).
doi: 10.1371/journal.ppat.1002237
Chandran, V. et al. Structure of the outer membrane complex of a type IV secretion system. Nature 462, 1011–1015 (2009).
pubmed: 19946264
pmcid: 2797999
doi: 10.1038/nature08588
Sgro, G. G. et al. CryoEM structure of the core complex of a bacterial killing type IV secretion system. Nat. Microbiol. 3, 1429–1440 (2018).
pubmed: 30349081
pmcid: 6264810
doi: 10.1038/s41564-018-0262-z
Chung, J. M. et al. Structure of the Helicobacter pylori Cag type IV secretion system. eLife 8, e47644 (2019).
pubmed: 31210639
pmcid: 6620104
doi: 10.7554/eLife.47644
Durie, C. L. et al. Structural analysis of the Legionella pneumophila Dot/Icm type IV secretion system core complex. eLife 9, e59530 (2020).
pubmed: 32876045
pmcid: 7511231
doi: 10.7554/eLife.59530
Sheedlo, M. J. et al. Cryo-EM reveals species-specific components within the Helicobacter pylori Cag type IV secretion system core complex. eLife 9, e59495 (2020).
pubmed: 32876048
pmcid: 7511236
doi: 10.7554/eLife.59495
Sheedlo, M. J. et al. Cryo-EM reveals new species-specific proteins and symmetry elements in the Legionella pneumophila Dot/Icm T4SS. eLife 10, e70427 (2021).
pubmed: 34519271
pmcid: 8486379
doi: 10.7554/eLife.70427
Fronzes, R. et al. Structure of a type IV secretion system core complex. Science 323, 266–268 (2009).
pubmed: 19131631
pmcid: 6710095
doi: 10.1126/science.1166101
Koraimann, G. Spread and persistence of virulence and antibiotic resistance genes: A ride on the F plasmid conjugation module. EcoSal Plus 8, https://doi.org/10.1128/ecosalplus.ESP-0003-2018 (2018).
Hu, B., Khara, P. & Christie, P. J. Structural bases for F plasmid conjugation and F pilus biogenesis in Escherichia coli. Proc. Natl. Acad. Sci USA 116, 14222–14227 (2019).
pubmed: 31239340
pmcid: 6628675
doi: 10.1073/pnas.1904428116
Fernandez, D. et al. The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface. J. Bacteriol. 178, 3156–3167 (1996).
pubmed: 8655494
pmcid: 178066
doi: 10.1128/jb.178.11.3156-3167.1996
McClain, M. S., Voss, B. J. & Cover, T. L. Lipoprotein processing and sorting in Helicobacter pylori. mBio 11, https://doi.org/10.1128/mBio.00911-20 (2020).
Arutyunov, D. & Frost, L. S. F conjugation: back to the beginning. Plasmid 70, 18–32 (2013).
pubmed: 23632276
doi: 10.1016/j.plasmid.2013.03.010
Cascales, E. & Christie, P. J. Agrobacterium VirB10, an ATP energy sensor required for type IV secretion. Proc. Natl. Acad. Sci. USA 101, 17228–17233 (2004).
pubmed: 15569944
pmcid: 535377
doi: 10.1073/pnas.0405843101
Cascales, E., Atmakuri, K., Sarkar, M. K. & Christie, P. J. DNA substrate-induced activation of the Agrobacterium VirB/VirD4 type IV secretion system. J. Bacteriol. 195, 2691–2704 (2013).
pubmed: 23564169
pmcid: 3676061
doi: 10.1128/JB.00114-13
Lawley, T. D., Klimke, W. A., Gubbins, M. J. & Frost, L. S. F factor conjugation is a true type IV secretion system. FEMS Microbiol. Lett 224, 1–15 (2003).
pubmed: 12855161
doi: 10.1016/S0378-1097(03)00430-0
Harris, R. L. & Silverman, P. M. Tra proteins characteristic of F-like type IV secretion systems constitute an interaction group by yeast two-hybrid analysis. J. Bacteriol. 186, 5480–5485 (2004).
pubmed: 15292150
pmcid: 490886
doi: 10.1128/JB.186.16.5480-5485.2004
Koch, B. et al. Protein interactions within and between two F-type type IV secretion systems. Mol Microbiol 114, 823–838 (2020).
pubmed: 32738086
pmcid: 8015186
doi: 10.1111/mmi.14582
Sagulenko, E., Sagulenko, V., Chen, J. & Christie, P. J. Role of Agrobacterium VirB11 ATPase in T-pilus assembly and substrate selection. J Bacteriol 183, 5813–5825 (2001).
pubmed: 11566978
pmcid: 99657
doi: 10.1128/JB.183.20.5813-5825.2001
Jakubowski, S. J., Cascales, E., Krishnamoorthy, V. & Christie, P. J. Agrobacterium tumefaciens VirB9, an outer-membrane-associated component of a type IV secretion system, regulates substrate selection and T-pilus biogenesis. J. Bacteriol. 187, 3486–3495 (2005).
pubmed: 15866936
pmcid: 1112014
doi: 10.1128/JB.187.10.3486-3495.2005
Christie, P. J., Atmakuri, K., Krishnamoorthy, V., Jakubowski, S. & Cascales, E. Biogenesis, architecture, and function of bacterial type IV secretion systems. Annu. Rev. Microbiol. 59, 451–485 (2005).
pubmed: 16153176
doi: 10.1146/annurev.micro.58.030603.123630
Worrall, L. J. et al. Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Nature 540, 597–601 (2016).
pubmed: 27974800
doi: 10.1038/nature20576
Hu, J. et al. Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. Nat. Commun. 9, 3840 (2018).
pubmed: 30242280
pmcid: 6155069
doi: 10.1038/s41467-018-06298-8
Chernyatina, A. A. & Low, H. H. Core architecture of a bacterial type II secretion system. Nat. Commun. 10, 5437 (2019).
pubmed: 31780649
pmcid: 6882859
doi: 10.1038/s41467-019-13301-3
Dix, S. R. et al. Structural insights into the function of type VI secretion system TssA subunits. Nat. Commun. 9, 4765 (2018).
pubmed: 30420757
pmcid: 6232143
doi: 10.1038/s41467-018-07247-1
Sobti, M. et al. Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch. Nat. Commun. 11, 2615 (2020).
pubmed: 32457314
pmcid: 7251095
doi: 10.1038/s41467-020-16387-2
Takekawa, N. et al. Two distinct conformations in 34 FliF subunits generate three different symmetries within the flagellar MS-Ring. mBio. 12, https://doi.org/10.1128/mBio.03199-20 (2021).
Thomason, L. C., Sawitzke, J. A., Li, X., Costantino, N. & Court, D. L. Recombineering: genetic engineering in bacteria using homologous recombination. Curr. Protoc. Mol. Biol. 106, 1.16.1–39 (2014).
doi: 10.1002/0471142727.mb0116s106
Swings, T. et al. CRISPR-FRT targets shared sites in a knock-out collection for off-the-shelf genome editing. Nat. Commun. 9, 2231 (2018).
pubmed: 29884781
pmcid: 5993718
doi: 10.1038/s41467-018-04651-5
Harb, L. et al. ssRNA phage penetration triggers detachment of the F-pilus. Proc. Natl. Acad. Sci. USA 117, 25751–25758 (2020).
pubmed: 32989140
pmcid: 7568308
doi: 10.1073/pnas.2011901117
Datsenko, K. A. & Wanner, B. L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97, 6640–6645 (2000).
pubmed: 10829079
pmcid: 18686
doi: 10.1073/pnas.120163297
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).
pubmed: 28165473
doi: 10.1038/nmeth.4169
Terwilliger, T. C., Sobolev, O. V., Afonine, P. V. & Adams, P. D. Automated map sharpening by maximization of detail and connectivity. Acta Crystallogr. D: Struct. Biol. 74, 545–559 (2018).
doi: 10.1107/S2059798318004655
Waterhouse, A. et al. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res. 46, W296–W303 (2018).
pubmed: 29788355
pmcid: 6030848
doi: 10.1093/nar/gky427
Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comp. Chem. 25, 1605–1612 (2004).
doi: 10.1002/jcc.20084
Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D: Biol. Crystallogr. 66, 486–501 (2010).
doi: 10.1107/S0907444910007493