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Bacterial killing via a type IV secretion system
Open accessAbstract
Type IV secretion systems (T4SSs) are multiprotein complexes that transport effector proteins and protein–DNA complexes through bacterial membranes to the extracellular milieu or directly into the cytoplasm of other cells. Many bacteria of the family Xanthomonadaceae, which occupy diverse environmental niches, carry a T4SS with unknown function but with several characteristics that distinguishes it from other T4SSs. Here we show that the Xanthomonas citri T4SS provides these cells the capacity to kill other Gram-negative bacterial species in a contact-dependent manner. The secretion of one type IV bacterial effector protein is shown to require a conserved C-terminal domain and its bacteriolytic activity is neutralized by a cognate immunity protein whose 3D structure is similar to peptidoglycan hydrolase inhibitors. This is the first demonstration of the involvement of a T4SS in bacterial killing and points to this special class of T4SS as a mediator of both antagonistic and cooperative interbacterial interactions. Bacterial secretion systems deliver proteins to the extracellular milieu or directly into the cytoplasm of other cells. Here Souza et al. show that a type IV secretion system (T4SS) allows Xanthomonas citrito kill other Gram-negative bacterial species in a contact-dependent manner.
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Cites
Sheldrick, G. M. (2008) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 87,804
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
REFMAC 5 for the refinement of macromolecular crystal structures
Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F., & Vagin, A. A. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911001314 · Cited by 8,317
Structure validation by Cα geometry: ϕ,ψ and Cβ deviation
Lovell, S. C., Davis, I. W., Arendall, W. B., de Bakker, P. I. W., Word, J. M., Prisant, M. G., Richardson, J. S., & Richardson, D. C. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10286 · Cited by 4,595
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,896
Svergun, D. I. (1992) · Journal of Applied Crystallography · doi:10.1107/s0021889892001663 · Cited by 3,759
Dali server: conservation mapping in 3D
Holm, L., & Rosenstr�m, P. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq366 · Cited by 3,640
Svergun, D., Barberato, C., & Koch, M. H. J. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,434
CDD: a Conserved Domain Database for the functional annotation of proteins
Marchler-Bauer, A., Lu, S., Anderson, J. B., Chitsaz, F., Derbyshire, M. K., DeWeese-Scott, C., Fong, J. H., Geer, L. Y., Geer, R. C., Gonzales, N. R., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1189 · Cited by 3,159
Svergun, D. I. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77443-6 · Cited by 2,221
Uniqueness of ab initio shape determination in small-angle scattering
Volkov, V. V., & Svergun, D. I. (2003) · Journal of Applied Crystallography · doi:10.1107/s0021889803000268 · Cited by 1,932
New developments in the ATSAS program package for small-angle scattering data analysis
Petoukhov, M. V., Franke, D., Shkumatov, A. V., Tria, G., Kikhney, A. G., Gajda, M., Gorba, C., Mertens, H. D. T., Konarev, P. V., & Svergun, D. I. (2012) · Journal of Applied Crystallography · doi:10.1107/s0021889812007662 · Cited by 1,903
Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
Langer, G., Cohen, S. X., Lamzin, V. S., & Perrakis, A. (2008) · Nature Protocols · doi:10.1038/nprot.2008.91 · Cited by 1,606
The finer things in X-ray diffraction data collection
Pflugrath, J. W. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744499900935x · Cited by 1,244
Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
Painter, J., & Merritt, E. A. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906005270 · Cited by 1,240
Comparison of the genomes of two Xanthomonas pathogens with differing host specificities
da Silva, A. C. R., Ferro, J. A., Reinach, F. C., Farah, C. S., Furlan, L. R., Quaggio, R. B., Monteiro-Vitorello, C. B., Sluys, M. A. V., Almeida, N. F., Alves, L. M. C., et al. (2002) · Nature · doi:10.1038/417459a · Cited by 1,218
Self-citationAutomated Structure Solution With autoSHARP
Vonrhein, C., Blanc, E., Roversi, P., & Bricogne, G. (2006) · Macromolecular Crystallography Protocols, Volume 2 · doi:10.1385/1-59745-266-1:215 · Cited by 963
A Type VI Secretion System of Pseudomonas aeruginosa Targets a Toxin to Bacteria
Hood, R. D., Singh, P., Hsu, F., Güvener, T., Carl, M. A., Trinidad, R. R. S., Silverman, J. M., Ohlson, B. B., Hicks, K. G., Plemel, R. L., et al. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.007 · Cited by 932
Biological Diversity of Prokaryotic Type IV Secretion Systems
Alvarez-Martinez, C. E., & Christie, P. J. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00023-09 · Cited by 729
Self-citationType VI secretion delivers bacteriolytic effectors to target cells
Russell, A. B., Hood, R. D., Bui, N. K., LeRoux, M., Vollmer, W., & Mougous, J. D. (2011) · Nature · doi:10.1038/nature10244 · Cited by 710
Tit-for-Tat: Type VI Secretion System Counterattack during Bacterial Cell-Cell Interactions
Basler, M., Ho, B. T., & Mekalanos, J. J. (2013) · Cell · doi:10.1016/j.cell.2013.01.042 · Cited by 556
Zhang, D., de Souza, R. F., Anantharaman, V., Iyer, L. M., & Aravind, L. (2012) · Biology Direct · doi:10.1186/1745-6150-7-18 · Cited by 515
Small‐angle scattering for structural biology—Expanding the frontier while avoiding the pitfalls
Jacques, D. A., & Trewhella, J. (2010) · Protein Science · doi:10.1002/pro.351 · Cited by 435
Diverse type VI secretion phospholipases are functionally plastic antibacterial effectors
Russell, A. B., LeRoux, M., Hathazi, K., Agnello, D. M., Ishikawa, T., Wiggins, P. A., Wai, S. N., & Mougous, J. D. (2013) · Nature · doi:10.1038/nature12074 · Cited by 414
The Vibrio cholerae type VI secretion system displays antimicrobial properties
MacIntyre, D. L., Miyata, S. T., Kitaoka, M., & Pukatzki, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012931107 · Cited by 409
Structure and Regulation of the Type VI Secretion System
Silverman, J. M., Brunet, Y. R., Cascales, E., & Mougous, J. D. (2012) · Annual Review of Microbiology · doi:10.1146/annurev-micro-121809-151619 · Cited by 402
Type IV secretion systems and their effectors in bacterial pathogenesis
Backert, S., & Meyer, T. F. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.02.008 · Cited by 378
Schwarz, S., West, T. E., Boyer, F., Chiang, W.-C., Carl, M. A., Hood, R. D., Rohmer, L., Tolker-Nielsen, T., Skerrett, S. J., & Mougous, J. D. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001068 · Cited by 374
Anantharaman, V., & Aravind, L. (2003) · Genome Biology · doi:10.1186/gb-2003-4-2-r11 · Cited by 365
Structural Perspective of Peptidoglycan Biosynthesis and Assembly
Lovering, A. L., Safadi, S. S., & Strynadka, N. C. J. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-112742 · Cited by 329
Structure of a Type IV Secretion System Core Complex
Fronzes, R., Schäfer, E., Wang, L., Saibil, H. R., Orlova, E. V., & Waksman, G. (2009) · Science · doi:10.1126/science.1166101 · Cited by 308
Structure of a type IV secretion system
Low, H. H., Gubellini, F., Rivera-Calzada, A., Braun, N., Connery, S., Dujeancourt, A., Lu, F., Redzej, A., Fronzes, R., Orlova, E. V., et al. (2014) · Nature · doi:10.1038/nature13081 · Cited by 303
Neisseria gonorrhoeae secretes chromosomal DNA via a novel type IV secretion system
Hamilton, H. L., Domínguez, N. M., Schwartz, K. J., Hackett, K. T., & Dillard, J. P. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04521.x · Cited by 295
Lytic transglycosylases: Bacterial space-making autolysins
Scheurwater, E., Reid, C. W., & Clarke, A. J. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.018 · Cited by 293
A Database of Bacterial Lipoproteins (DOLOP) with Functional Assignments to Predicted Lipoproteins
Babu, M. M., Priya, M. L., Selvan, A. T., Madera, M., Gough, J., Aravind, L., & Sankaran, K. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.8.2761-2773.2006 · Cited by 293
Barbosa, L. R. S., Ortore, M. G., Spinozzi, F., Mariani, P., Bernstorff, S., & Itri, R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.09.056 · Cited by 281
Self-citationPitzschke, A., & Hirt, H. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.8 · Cited by 274
TopDraw: a sketchpad for protein structure topology cartoons
Bond, C. S. (2003) · Bioinformatics · doi:10.1093/bioinformatics/19.2.311 · Cited by 259
Tegtmeyer, N., Wessler, S., & Backert, S. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08035.x · Cited by 250
Casas-Godoy, L., Duquesne, S., Bordes, F., Sandoval, G., & Marty, A. (2012) · Methods in Molecular Biology · doi:10.1007/978-1-61779-600-5_1 · Cited by 243
Murdoch, S. L., Trunk, K., English, G., Fritsch, M. J., Pourkarimi, E., & Coulthurst, S. J. (2011) · Journal of Bacteriology · doi:10.1128/jb.05671-11 · Cited by 238
Hofreuter, D., Odenbreit, S., & Haas, R. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02502.x · Cited by 238
Mutschler, H., Gebhardt, M., Shoeman, R. L., & Meinhart, A. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001033 · Cited by 231
Type II secretion system: A magic beanstalk or a protein escalator
Nivaskumar, M., & Francetic, O. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.12.020 · Cited by 200
Zhang, D., Iyer, L. M., & Aravind, L. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr036 · Cited by 197
Marker for type VI secretion system effectors
Salomon, D., Kinch, L. N., Trudgian, D. C., Guo, X., Klimko, J. A., Grishin, N. V., Mirzaei, H., & Orth, K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406110111 · Cited by 191
The ins and outs of pertussis toxin
Locht, C., Coutte, L., & Mielcarek, N. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08237.x · Cited by 190
Bacterial chitinases and chitin-binding proteins as virulence factors
Frederiksen, R. F., Paspaliari, D. K., Larsen, T., Storgaard, B. G., Larsen, M. H., Ingmer, H., Palcic, M. M., & Leisner, J. J. (2013) · Microbiology · doi:10.1099/mic.0.051839-0 · Cited by 187
Assembly and structure of the T3SS
Burkinshaw, B. J., & Strynadka, N. C. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.01.035 · Cited by 164
Type 6 Secretion System–Mediated Immunity to Type 4 Secretion System–Mediated Gene Transfer
Ho, B. T., Basler, M., & Mekalanos, J. J. (2013) · Science · doi:10.1126/science.1243745 · Cited by 139
Type V secretion: From biogenesis to biotechnology
van Ulsen, P., Rahman, S. U., Jong, W. S. P., Daleke, M. H., & Luirink, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.006 · Cited by 126
Wohlkönig, A., Huet, J., Looze, Y., & Wintjens, R. T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015388 · Cited by 122
Dehio, C. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01171.x · Cited by 105
Mechanisms and Biological Roles of Contact-Dependent Growth Inhibition SystemsPreprint
Hayes, C. S., Koskiniemi, S., Ruhe, Z. C., Poole, S. J., & Low, D. A. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a010025 · Cited by 102
Alegria, M. C., de Souza, D. P., Andrade, M. O., Docena, C., Khater, L., Ramos, C. H. I., da Silva, A. C. R., & Farah, C. S. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.7.2315-2325.2005 · Cited by 95
Self-citationRecent advances in the structural and molecular biology of type IV secretion systems
Trokter, M., Felisberto‐Rodrigues, C., Christie, P. J., & Waksman, G. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.02.006 · Cited by 90
Folds and activities of peptidoglycan amidases
Firczuk, M., & Bochtler, M. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00084.x · Cited by 81
de Souza, D. P., Andrade, M. O., Alvarez‐Martinez, C. E., Arantes, G. M., Farah, C. S., & Salinas, R. K. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002031 · Cited by 76
Self-citationManipulation of host vesicular trafficking and innate immune defence by Legionella Dot/Icm effectors
Ge, J., & Shao, F. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01710.x · Cited by 69
Ding, J., Wang, W., Han, F., Zhang, Y., & Wang, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.368043 · Cited by 48
Lysozyme inhibitor conferring bacterial tolerance to invertebrate type lysozyme
Herreweghe, J. M. V., Vanderkelen, L., Callewaert, L., Aertsen, A., Compernolle, G., Declerck, P. J., & Michiels, C. W. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0241-x · Cited by 45
Structural organisation of the type IV secretion systems
Waksman, G., & Orlova, E. V. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.11.001 · Cited by 34
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Metadata
- Authors
- Souza, D. P., Oka, G. U., Alvarez-Martinez, C. E., Bisson-Filho, A. W., Dunger, G., Hobeika, L., Cavalcante, N. S., Alegria, M. C., Barbosa, L. R. S., Salinas, R. K., Guzzo, C. R., & Farah, C. S.
- Venue
- Nature Communications
- Published
- 2015-03-06
- Volume
- 6
- Issue
- 1
- Pages
- 6453-6453
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2073690728
- Cited by
- 271
- References
- 65
- FWCI
- 9.25
- Type
- journal article
- Language
- en
- Open access
- gold
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