Silence as a way of niche adaptation: mecC-MRSA with variations in the accessory gene regulator (agr) functionality express kaleidoscopic phenotypes.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
08 09 2020
Historique:
received: 10 12 2019
accepted: 19 08 2020
entrez: 9 9 2020
pubmed: 10 9 2020
medline: 27 3 2021
Statut: epublish

Résumé

Functionality of the accessory gene regulator (agr) quorum sensing system is an important factor promoting either acute or chronic infections by the notorious opportunistic human and veterinary pathogen Staphylococcus aureus. Spontaneous alterations of the agr system are known to frequently occur in human healthcare-associated S. aureus lineages. However, data on agr integrity and function are sparse regarding other major clonal lineages. Here we report on the agr system functionality and activity level in mecC-carrying methicillin resistant S. aureus (MRSA) of various animal origins (n = 33) obtained in Europe as well as in closely related human isolates (n = 12). Whole genome analysis assigned all isolates to four clonal complexes (CC) with distinct agr types (CC599 agr I, CC49 agr II, CC130 agr III and CC1943 agr IV). Agr functionality was assessed by a combination of phenotypic assays and proteome analysis. In each CC, isolates with varying agr activity levels were detected, including the presence of completely non-functional variants. Genomic comparison of the agr I-IV encoding regions associated these phenotypic differences with variations in the agrA and agrC genes. The genomic changes were detected independently in divergent lineages, suggesting that agr variation might foster viability and adaptation of emerging MRSA lineages to distinct ecological niches.

Identifiants

pubmed: 32901059
doi: 10.1038/s41598-020-71640-4
pii: 10.1038/s41598-020-71640-4
pmc: PMC7479134
doi:

Substances chimiques

Agr protein, Staphylococcus aureus 0
Bacterial Proteins 0
Hemolysin Proteins 0
Proteome 0
Trans-Activators 0
Virulence Factors 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

14787

Références

Walther, B. et al. Equine methicillin-resistant sequence type 398 Staphylococcus aureus (MRSA) harbor mobile genetic elements promoting host adaptation. Front. Microbiol. 9, 2516. https://doi.org/10.3389/fmicb.2018.02516 (2018).
doi: 10.3389/fmicb.2018.02516 pubmed: 30405574 pmcid: 6207647
Lowy, F. D. Staphylococcus aureus infections. N. Engl. J. Med. 339, 520–532. https://doi.org/10.1056/nejm199808203390806 (1998).
doi: 10.1056/nejm199808203390806 pubmed: 9709046
Kriegeskorte, A. & Peters, G. Horizontal gene transfer boosts MRSA spreading. Nat. Med. 18, 662–663. https://doi.org/10.1038/nm.2765 (2012).
doi: 10.1038/nm.2765 pubmed: 22561821
Peacock, S. J. & Paterson, G. K. Mechanisms of methicillin resistance in Staphylococcus aureus. Annu. Rev. Biochem. 84, 577–601. https://doi.org/10.1146/annurev-biochem-060614-034516 (2015).
doi: 10.1146/annurev-biochem-060614-034516 pubmed: 26034890
Garcia-Alvarez, L. et al. Meticillin-resistant Staphylococcus aureus with a novel mecA homologue in human and bovine populations in the UK and Denmark: a descriptive study. Lancet Infect. Dis. 11, 595–603. https://doi.org/10.1016/s1473-3099(11)70126-8 (2011).
doi: 10.1016/s1473-3099(11)70126-8 pubmed: 21641281 pmcid: 3829197
Baig, S. et al. Novel SCCmec type XIII (9A) identified in an ST152 methicillin-resistant Staphylococcus aureus. Infect. Genet. Evol. 61, 74–76. https://doi.org/10.1016/j.meegid.2018.03.013 (2018).
doi: 10.1016/j.meegid.2018.03.013 pubmed: 29567305
Kerschner, H., Harrison, E. M., Hartl, R., Holmes, M. A. & Apfalter, P. First report of mecC MRSA in human samples from Austria: molecular characteristics and clinical data. New Microb. New Infect. 3, 4–9. https://doi.org/10.1016/j.nmni.2014.11.001 (2015).
doi: 10.1016/j.nmni.2014.11.001
Paterson, G. K., Harrison, E. M. & Holmes, M. A. The emergence of mecC methicillin-resistant Staphylococcus aureus. Trends Microbiol. 22, 42–47. https://doi.org/10.1016/j.tim.2013.11.003 (2014).
doi: 10.1016/j.tim.2013.11.003 pubmed: 24331435 pmcid: 3989053
Cuny, C., Layer, F., Strommenger, B. & Witte, W. Rare occurrence of methicillin-resistant Staphylococcus aureus CC130 with a novel mecA homologue in humans in Germany. PLoS ONE 6, e24360. https://doi.org/10.1371/journal.pone.0024360 (2011).
doi: 10.1371/journal.pone.0024360 pubmed: 21931689 pmcid: 3169590
Ford, B. A. mecC-harboring methicillin-resistant Staphylococcus aureus: hiding in plain sight. J. Clin. Microbiol. 5, 6. https://doi.org/10.1128/jcm.01549-17 (2018).
doi: 10.1128/jcm.01549-17
Kil, E. H., Heymann, W. R. & Weinberg, J. M. Methicillin-resistant Staphylococcus aureus: an update for the dermatologist, part 4: additional therapeutic considerations. Cutis 81, 343–347 (2008).
pubmed: 18491483
Shore, A. C. et al. Detection of staphylococcal cassette chromosome mec type XI carrying highly divergent mecA, mecI, mecR1, blaZ, and ccr genes in human clinical isolates of clonal complex 130 methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 55, 3765–3773. https://doi.org/10.1128/aac.00187-11 (2011).
doi: 10.1128/aac.00187-11 pubmed: 21636525 pmcid: 3147645
Worthing, K. A. et al. Isolation of mecC MRSA in Australia. J. Antimicrob. Chemother. 71, 2348–2349. https://doi.org/10.1093/jac/dkw138 (2016).
doi: 10.1093/jac/dkw138 pubmed: 27118772
Walther, B. et al. MRSA variant in companion animals. Emerg. Infect. Dis. 18, 2017–2020. https://doi.org/10.3201/eid1812.120238 (2012).
doi: 10.3201/eid1812.120238 pubmed: 23171478 pmcid: 3557870
Loncaric, I. et al. Characterization of methicillin-resistant Staphylococcus spp. carrying the mecC gene, isolated from wildlife. J. Antimicrob. Chemother. 68, 2222–2225. https://doi.org/10.1093/jac/dkt186 (2013).
doi: 10.1093/jac/dkt186 pubmed: 23674764
Garcia-Garrote, F. et al. Methicillin-resistant Staphylococcus aureus carrying the mecC gene: emergence in Spain and report of a fatal case of bacteraemia. J. Antimicrob. Chemother. 69, 45–50. https://doi.org/10.1093/jac/dkt327 (2014).
doi: 10.1093/jac/dkt327 pubmed: 23975743
Mekonnen, S. A. et al. Metabolic niche adaptation of community- and hospital-associated methicillin-resistant Staphylococcus aureus. J. Proteom. 193, 154–161. https://doi.org/10.1016/j.jprot.2018.10.005 (2019).
doi: 10.1016/j.jprot.2018.10.005
Paharik, A. E. & Horswill, A. R. The Staphylococcal biofilm: adhesins, regulation, and host response. Microbiol. Spectr. https://doi.org/10.1128/microbiolspec.VMBF-0022-2015 (2016).
doi: 10.1128/microbiolspec.VMBF-0022-2015 pubmed: 27227309 pmcid: 4887152
Hammer, N. D. & Skaar, E. P. Molecular mechanisms of Staphylococcus aureus iron acquisition. Annu. Rev. Microbiol. 65, 129–147. https://doi.org/10.1146/annurev-micro-090110-102851 (2011).
doi: 10.1146/annurev-micro-090110-102851 pubmed: 21639791
Lerat, E. & Ochman, H. Recognizing the pseudogenes in bacterial genomes. Nucl. Acids Res. 33, 3125–3132. https://doi.org/10.1093/nar/gki631 (2005).
doi: 10.1093/nar/gki631 pubmed: 15933207
Mcgavin, M., Arsic, B. & Nickerson, N. Evolutionary blueprint for host- and niche-adaptation in Staphylococcus aureus clonal complex CC30. Front. Cell. Infect. Microbiol. https://doi.org/10.3389/fcimb.2012.00048 (2012).
doi: 10.3389/fcimb.2012.00048 pubmed: 22919657 pmcid: 3417565
Tavares, A. et al. Insights into alpha-hemolysin (Hla) evolution and expression among Staphylococcus aureus clones with hospital and community origin. PLoS ONE 9, e98634. https://doi.org/10.1371/journal.pone.0098634 (2014).
doi: 10.1371/journal.pone.0098634 pubmed: 25033196 pmcid: 4102472
Yoong, P. & Torres, V. J. Counter inhibition between leukotoxins attenuates Staphylococcus aureus virulence. Nat. Commun. 6, 8125. https://doi.org/10.1038/ncomms9125 (2015).
doi: 10.1038/ncomms9125 pubmed: 26330208 pmcid: 4562310
Chadha, A. D. et al. Host response to Staphylococcus aureus cytotoxins in children with cystic fibrosis. J. Cyst. Fibros. Off. J. Eur. Cyst. Fibros. Soc. 15, 597–604. https://doi.org/10.1016/j.jcf.2015.12.023 (2016).
doi: 10.1016/j.jcf.2015.12.023
Benson, M. A. et al. Evolution of hypervirulence by a MRSA clone through acquisition of a transposable element. Mol. Microbiol. 93, 664–681. https://doi.org/10.1111/mmi.12682 (2014).
doi: 10.1111/mmi.12682 pubmed: 24962815 pmcid: 4127135
Busche, T. et al. Comparative secretome analyses of human and zoonotic Staphylococcus aureus Isolates CC8, CC22, and CC398. Mol. Cell. Proteom. MCP 17, 2412–2433. https://doi.org/10.1074/mcp.RA118.001036 (2018).
doi: 10.1074/mcp.RA118.001036
Richardson, E. J. et al. Gene exchange drives the ecological success of a multi-host bacterial pathogen. Nat. Ecol. Evol. 2, 1468–1478. https://doi.org/10.1038/s41559-018-0617-0 (2018).
doi: 10.1038/s41559-018-0617-0 pubmed: 30038246
Walther, B. et al. Comparative molecular analysis substantiates zoonotic potential of equine methicillin-resistant Staphylococcus aureus. J. Clin. Microbiol. 47, 704–710. https://doi.org/10.1128/jcm.01626-08 (2009).
doi: 10.1128/jcm.01626-08 pubmed: 19109463
Wang, B. & Muir, T. W. Regulation of virulence in Staphylococcus aureus: molecular mechanisms and remaining puzzles. Cell Chem. Biol. 23, 214–224. https://doi.org/10.1016/j.chembiol.2016.01.004 (2016).
doi: 10.1016/j.chembiol.2016.01.004 pubmed: 26971873 pmcid: 4847544
Jenul, C. & Horswill, A. R. Regulation of Staphylococcus aureus virulence. Microbiol. Spectr. https://doi.org/10.1128/microbiolspec.GPP3-0031-2018 (2018).
doi: 10.1128/microbiolspec.GPP3-0031-2018 pubmed: 30953424 pmcid: 6452892
Cheung, A. L. et al. Diminished virulence of a sar-/agr-mutant of Staphylococcus aureus in the rabbit model of endocarditis. J. Clin. Investig. 94, 1815–1822. https://doi.org/10.1172/jci117530 (1994).
doi: 10.1172/jci117530 pubmed: 7962526
Kobayashi, S. D. et al. Comparative analysis of USA300 virulence determinants in a rabbit model of skin and soft tissue infection. J. Infect. Dis. 204, 937–941. https://doi.org/10.1093/infdis/jir441 (2011).
doi: 10.1093/infdis/jir441 pubmed: 21849291 pmcid: 3156927
Abdelnour, A., Arvidson, S., Bremell, T., Rydén, C. & Tarkowski, A. The accessory gene regulator (agr) controls Staphylococcus aureus virulence in a murine arthritis model. Infect. Immun. 61, 3879–3885 (1993).
doi: 10.1128/IAI.61.9.3879-3885.1993
Fowler, V. G. Jr. et al. Persistent bacteremia due to methicillin-resistant Staphylococcus aureus infection is associated with agr dysfunction and low-level in vitro resistance to thrombin-induced platelet microbicidal protein. J. Infect. Dis. 190, 1140–1149. https://doi.org/10.1086/423145 (2004).
doi: 10.1086/423145 pubmed: 15319865
Traber, K. E. et al. agr function in clinical Staphylococcus aureus isolates. Microbiology (Reading, England) 154, 2265–2274. https://doi.org/10.1099/mic.0.2007/011874-0 (2008).
doi: 10.1099/mic.0.2007/011874-0
Schweizer, M. L. et al. Increased mortality with accessory gene regulator (agr) dysfunction in Staphylococcus aureus among bacteremic patients. Antimicrob. Agents Chemother. 55, 1082–1087. https://doi.org/10.1128/aac.00918-10 (2011).
doi: 10.1128/aac.00918-10 pubmed: 21173172
Painter, K. L., Krishna, A., Wigneshweraraj, S. & Edwards, A. M. What role does the quorum-sensing accessory gene regulator system play during Staphylococcus aureus bacteremia?. Trends Microbiol. 22, 676–685. https://doi.org/10.1016/j.tim.2014.09.002 (2014).
doi: 10.1016/j.tim.2014.09.002 pubmed: 25300477
Yang, X. et al. Accessory gene regulator (agr) dysfunction was unusual in Staphylococcus aureus isolated from Chinese children. BMC Microbiol. 19, 95. https://doi.org/10.1186/s12866-019-1465-z (2019).
doi: 10.1186/s12866-019-1465-z pubmed: 31088356 pmcid: 6518674
He, L. et al. Resistance to leukocytes ties benefits of quorum sensing dysfunctionality to biofilm infection. Nat. Microbiol. 4, 1114–1119. https://doi.org/10.1038/s41564-019-0413-x (2019).
doi: 10.1038/s41564-019-0413-x pubmed: 6588452 pmcid: 6588452
Altman, D. R. et al. Genome plasticity of agr-defective Staphylococcus aureus during clinical infection. Infect. Immun. https://doi.org/10.1128/iai.00331-18 (2018).
doi: 10.1128/iai.00331-18 pubmed: 30242013 pmcid: 6204747
Goerke, C. et al. Direct quantitative transcript analysis of the agr regulon of Staphylococcus aureus during human infection in comparison to the expression profile in vitro. Infect. Immun. 68, 1304–1311. https://doi.org/10.1128/iai.68.3.1304-1311.2000 (2000).
doi: 10.1128/iai.68.3.1304-1311.2000 pubmed: 10678942 pmcid: 97283
Suligoy, C. M. et al. Mutation of Agr is associated with the adaptation of Staphylococcus aureus to the host during chronic osteomyelitis. Front. Cell. Infect. Microbiol. 8, 18. https://doi.org/10.3389/fcimb.2018.00018 (2018).
doi: 10.3389/fcimb.2018.00018 pubmed: 29456969 pmcid: 5801681
Le, K. Y. & Otto, M. Quorum-sensing regulation in staphylococci—an overview. Front. Microbiol. 6, 1174. https://doi.org/10.3389/fmicb.2015.01174 (2015).
doi: 10.3389/fmicb.2015.01174 pubmed: 26579084 pmcid: 4621875
Reynolds, J. & Wigneshweraraj, S. Molecular insights into the control of transcription initiation at the Staphylococcus aureus agr operon. J. Mol. Biol. 412, 862–881. https://doi.org/10.1016/j.jmb.2011.06.018 (2011).
doi: 10.1016/j.jmb.2011.06.018 pubmed: 21741390
Abisado, R. G., Benomar, S., Klaus, J. R., Dandekar, A. A. & Chandler, J. R. Bacterial quorum sensing and microbial community interactions. mBio 9, e02331-02317. https://doi.org/10.1128/mBio.02331-17 (2018).
doi: 10.1128/mBio.02331-17
Benito, Y. et al. Probing the structure of RNAIII, the Staphylococcus aureus agr regulatory RNA, and identification of the RNA domain involved in repression of protein A expression. RNA (New York, N.Y.) 6, 668–679. https://doi.org/10.1017/s1355838200992550 (2000).
doi: 10.1017/s1355838200992550
Joo, H. S. et al. Mechanism of gene regulation by a Staphylococcus aureus toxin. mBio https://doi.org/10.1128/mBio.01579-16 (2016).
doi: 10.1128/mBio.01579-16 pubmed: 27795396 pmcid: 5080381
Cheung, G. Y., Wang, R., Khan, B. A., Sturdevant, D. E. & Otto, M. Role of the accessory gene regulator agr in community-associated methicillin-resistant Staphylococcus aureus pathogenesis. Infect. Immun. 79, 1927–1935. https://doi.org/10.1128/iai.00046-11 (2011).
doi: 10.1128/iai.00046-11 pubmed: 21402769 pmcid: 3088142
Fisher, E. L., Otto, M. & Cheung, G. Y. C. Basis of Virulence in enterotoxin-mediated staphylococcal food poisoning. Front. Microbiol. https://doi.org/10.3389/fmicb.2018.00436 (2018).
doi: 10.3389/fmicb.2018.00436 pubmed: 30294314 pmcid: 6158360
Ferreira, F. A. et al. Impact of agr dysfunction on virulence profiles and infections associated with a novel methicillin-resistant Staphylococcus aureus (MRSA) variant of the lineage ST1-SCCmec IV. BMC Microbiol. 13, 93. https://doi.org/10.1186/1471-2180-13-93 (2013).
doi: 10.1186/1471-2180-13-93 pubmed: 23622558 pmcid: 3652751
Tasse, J. et al. Association between biofilm formation phenotype and clonal lineage in Staphylococcus aureus strains from bone and joint infections. PLoS ONE 13, e0200064. https://doi.org/10.1371/journal.pone.0200064 (2018).
doi: 10.1371/journal.pone.0200064 pubmed: 30161132 pmcid: 6116976
Jang, H. C. et al. Difference in agr dysfunction and reduced vancomycin susceptibility between MRSA bacteremia involving SCCmec types IV/IVa and I-III. PLoS ONE 7, e49136. https://doi.org/10.1371/journal.pone.0049136 (2012).
doi: 10.1371/journal.pone.0049136 pubmed: 23152862 pmcid: 3495764
Sheppard, S. K., Guttman, D. S. & Fitzgerald, J. R. Population genomics of bacterial host adaptation. Nat. Rev. Genet. 19, 549–565. https://doi.org/10.1038/s41576-018-0032-z (2018).
doi: 10.1038/s41576-018-0032-z pubmed: 29973680
Merlino, J. et al. Detection and expression of methicillin/oxacillin resistance in multidrug-resistant and non-multidrug-resistant Staphylococcus aureus in Central Sydney Australia. J. Antimicrob. Chemother. 49, 793–801 (2002).
doi: 10.1093/jac/dkf021
Clinical and Laboratory Standards Institute. Performance Standards for Antimicrobial Susceptibility Testing: Twenty-Fourth Informational Supplement M100-S24 (2014).
Clinical and Laboratory Standards Institute (Wayne, PA, 2013).
Bankevich, A. et al. SPAdes: a new genome assembly algorithm and its applications to single-cell sequencing. J. Comput. Biol. J. Comput. Mol. Cell Biol. 19, 455–477. https://doi.org/10.1089/cmb.2012.0021 (2012).
doi: 10.1089/cmb.2012.0021
Seemann, T. Prokka: rapid prokaryotic genome annotation. Bioinformatics 30, 2068–2069. https://doi.org/10.1093/bioinformatics/btu153 (2014).
doi: 10.1093/bioinformatics/btu153 pubmed: 24642063
Larsen, M. V. et al. Multilocus sequence typing of total-genome-sequenced bacteria. J. Clin. Microbiol. 50, 1355–1361. https://doi.org/10.1128/jcm.06094-11 (2012).
doi: 10.1128/jcm.06094-11 pubmed: 22238442 pmcid: 3318499
Kearse, M. et al. Geneious basic: an integrated and extendable desktop software platform for the organization and analysis of sequence data. Bioinformatics 28, 1647–1649. https://doi.org/10.1093/bioinformatics/bts199 (2012).
doi: 10.1093/bioinformatics/bts199 pubmed: 3371832 pmcid: 3371832
Zankari, E. et al. Identification of acquired antimicrobial resistance genes. J. Antimicrob. Chemother. 67, 2640–2644. https://doi.org/10.1093/jac/dks261 (2012).
doi: 10.1093/jac/dks261 pubmed: 22782487 pmcid: 3468078
Joensen, K. G. et al. Real-time whole-genome sequencing for routine typing, surveillance, and outbreak detection of verotoxigenic Escherichia coli. J. Clin. Microbiol. 52, 1501–1510. https://doi.org/10.1128/jcm.03617-13 (2014).
doi: 10.1128/jcm.03617-13 pubmed: 24574290 pmcid: 3993690
Bartels, M. D. et al. Comparing whole-genome sequencing with Sanger sequencing for spa typing of methicillin-resistant Staphylococcus aureus. J. Clin. Microbiol. 52, 4305–4308. https://doi.org/10.1128/jcm.01979-14 (2014).
doi: 10.1128/jcm.01979-14 pubmed: 25297335 pmcid: 4313303
von Mentzer, A. et al. Identification of enterotoxigenic Escherichia coli (ETEC) clades with long-term global distribution. Nat. Genet. 46, 1321. https://doi.org/10.1038/ng.3145 (2015).
doi: 10.1038/ng.3145
Stamatakis, A. RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies. Bioinformatics (Oxford, England) 30, 1312–1313. https://doi.org/10.1093/bioinformatics/btu033 (2014).
doi: 10.1093/bioinformatics/btu033
Hadfield, J. et al. Phandango: an interactive viewer for bacterial population genomics. Bioinformatics https://doi.org/10.1093/bioinformatics/btx610 (2017).
doi: 10.1093/bioinformatics/btx610 pmcid: 5860215
Cheung, G. Y. C., Duong, A. C. & Otto, M. Direct and synergistic hemolysis caused by Staphylococcus phenol-soluble modulins: implications for diagnosis and pathogenesis. Microbes Infect. 14, 380–386. https://doi.org/10.1016/j.micinf.2011.11.013 (2012).
doi: 10.1016/j.micinf.2011.11.013 pubmed: 22178792
Nair, D. et al. Whole-genome sequencing of Staphylococcus aureus strain RN4220, a key laboratory strain used in virulence research, identifies mutations that affect not only virulence factors but also the fitness of the strain. J. Bacteriol. 193, 2332–2335. https://doi.org/10.1128/jb.00027-11 (2011).
doi: 10.1128/jb.00027-11 pubmed: 21378186 pmcid: 3133102
Montgomery, C. P., Boyle-Vavra, S. & Daum, R. S. Importance of the global regulators Agr and SaeRS in the pathogenesis of CA-MRSA USA300 infection. PLoS ONE 5, e15177. https://doi.org/10.1371/journal.pone.0015177 (2010).
doi: 10.1371/journal.pone.0015177 pubmed: 21151999 pmcid: 2996312
Gase, K., Ferretti, J. J., Primeaux, C. & McShan, W. M. Identification, cloning, and expression of the CAMP factor gene (cfa) of group A streptococci. Infect. Immun. 67, 4725–4731 (1999).
doi: 10.1128/IAI.67.9.4725-4731.1999
Kaito, C. & Sekimizu, K. Colony spreading in Staphylococcus aureus. J. Bacteriol. 189, 2553–2557. https://doi.org/10.1128/JB.01635-06 (2007).
doi: 10.1128/JB.01635-06 pubmed: 17194792
Tsompanidou, E. et al. Requirement of the agr locus for colony spreading of Staphylococcus aureus. J. Bacteriol. 193, 1267–1272. https://doi.org/10.1128/jb.01276-10 (2011).
doi: 10.1128/jb.01276-10 pubmed: 21169484
Lin, M.-H., Ke, W.-J., Liu, C.-C. & Yang, M.-W. Modulation of Staphylococcus aureus spreading by water. Sci. Rep. 6, 25233. https://doi.org/10.1038/srep25233 (2016).
doi: 10.1038/srep25233 pubmed: 27125382 pmcid: 4850448
Tsompanidou, E. et al. The sortase A substrates FnbpA, FnbpB, ClfA and ClfB antagonize colony spreading of Staphylococcus aureus. PLoS ONE 7, e44646. https://doi.org/10.1371/journal.pone.0044646 (2012).
doi: 10.1371/journal.pone.0044646 pubmed: 22970276 pmcid: 3436756
Doellinger, J., Schneider, A., Hoeller, M. & Lasch, P. Sample preparation by easy extraction and digestion (SPEED)—a universal, rapid, and detergent-free protocol for proteomics based on acid extraction. Mol. Cell. Proteom. MCP https://doi.org/10.1074/mcp.TIR119.001616 (2019).
doi: 10.1074/mcp.TIR119.001616
Rappsilber, J., Mann, M. & Ishihama, Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896–1906. https://doi.org/10.1038/nprot.2007.261 (2007).
doi: 10.1038/nprot.2007.261 pubmed: 17703201
Demichev, V., Messner, C. B., Vernardis, S. I., Lilley, K. S. & Ralser, M. DIA-NN: neural networks and interference correction enable deep proteome coverage in high throughput. Nat. Methods https://doi.org/10.1038/s41592-019-0638-x (2019).
doi: 10.1038/s41592-019-0638-x pubmed: 31768060 pmcid: 6949130
Christensen, G. D. et al. Adherence of coagulase-negative staphylococci to plastic tissue culture plates: a quantitative model for the adherence of staphylococci to medical devices. J. Clin. Microbiol. 22, 996–1006 (1985).
doi: 10.1128/JCM.22.6.996-1006.1985
Becker, K., Ballhausen, B., Köck, R. & Kriegeskorte, A. Methicillin resistance in Staphylococcus isolates: the “mec alphabet” with specific consideration of mecC, a mec homolog associated with zoonotic S. aureus lineages. Int. J. Med. Microbiol. 304, 794–804. https://doi.org/10.1016/j.ijmm.2014.06.007 (2014).
doi: 10.1016/j.ijmm.2014.06.007 pubmed: 25034857
Fitzgerald, J. R. et al. Characterization of a putative pathogenicity island from bovine Staphylococcus aureus encoding multiple superantigens. J. Bacteriol. 183, 63–70. https://doi.org/10.1128/jb.183.1.63-70.2001 (2001).
doi: 10.1128/jb.183.1.63-70.2001 pubmed: 11114901 pmcid: 94850
Bosi, E. et al. Comparative genome-scale modelling of Staphylococcus aureus strains identifies strain-specific metabolic capabilities linked to pathogenicity. Proc. Natl. Acad. Sci. USA 113, E3801-3809. https://doi.org/10.1073/pnas.1523199113 (2016).
doi: 10.1073/pnas.1523199113 pubmed: 27286824
Monecke, S. et al. Detection of mecC-positive Staphylococcus aureus (CC130-MRSA-XI) in diseased European hedgehogs (Erinaceus europaeus) in Sweden. PLoS ONE 8, e66166. https://doi.org/10.1371/journal.pone.0066166 (2013).
doi: 10.1371/journal.pone.0066166 pubmed: 23776626 pmcid: 3680430
Shopsin, B. et al. Prevalence of agr specificity groups among Staphylococcus aureus strains colonizing children and their guardians. J. Clin. Microbiol. 41, 456–459. https://doi.org/10.1128/jcm.41.1.456-459.2003 (2003).
doi: 10.1128/jcm.41.1.456-459.2003 pubmed: 12517893 pmcid: 149583
Queck, S. Y. et al. RNAIII-independent target gene control by the agr quorum-sensing system: insight into the evolution of virulence regulation in Staphylococcus aureus. Mol. Cell 32, 150–158. https://doi.org/10.1016/j.molcel.2008.08.005 (2008).
doi: 10.1016/j.molcel.2008.08.005 pubmed: 18851841 pmcid: 2575650
Morrison, J. M., Anderson, K. L., Beenken, K. E., Smeltzer, M. S. & Dunman, P. M. The staphylococcal accessory regulator, SarA, is an RNA-binding protein that modulates the mRNA turnover properties of late-exponential and stationary phase Staphylococcus aureus cells. Front. Cell. Infect. Microbiol. 2, 26. https://doi.org/10.3389/fcimb.2012.00026 (2012).
doi: 10.3389/fcimb.2012.00026 pubmed: 22919618 pmcid: 3417590
Traber, K. & Novick, R. A slipped-mispairing mutation in AgrA of laboratory strains and clinical isolates results in delayed activation of agr and failure to translate δ- and α-haemolysins. Mol. Microbiol. 59, 1519–1530. https://doi.org/10.1111/j.1365-2958.2006.04986.x (2006).
doi: 10.1111/j.1365-2958.2006.04986.x pubmed: 16468992
Vincze, S. et al. Alarming proportions of methicillin-resistant Staphylococcus aureus (MRSA) in wound samples from companion animals, Germany 2010–2012. PLoS ONE 9, e85656. https://doi.org/10.1371/journal.pone.0085656 (2014).
doi: 10.1371/journal.pone.0085656 pubmed: 24465637 pmcid: 3896405
Kaspar, U. et al. Zoonotic multidrug-resistant microorganisms among small companion animals in Germany. PLoS ONE 13, e0208364. https://doi.org/10.1371/journal.pone.0208364 (2018).
doi: 10.1371/journal.pone.0208364 pubmed: 30532196 pmcid: 6285998
Sidote, D. J., Barbieri, C. M., Wu, T. & Stock, A. M. Structure of the Staphylococcus aureus AgrA LytTR domain bound to DNA reveals a beta fold with an unusual mode of binding. Structure 16, 727–735. https://doi.org/10.1016/j.str.2008.02.011 (2008).
doi: 10.1016/j.str.2008.02.011 pubmed: 18462677 pmcid: 2430735
George Cisar, E. A., Geisinger, E., Muir, T. W. & Novick, R. P. Symmetric signalling within asymmetric dimers of the Staphylococcus aureus receptor histidine kinase AgrC. Mol. Microbiol. 74, 44–57. https://doi.org/10.1111/j.1365-2958.2009.06849.x (2009).
doi: 10.1111/j.1365-2958.2009.06849.x pubmed: 19708918 pmcid: 3913215
Recsei, P. et al. Regulation of exoprotein gene expression in Staphylococcus aureus by agar. Mol. Gen. Genet. MGG 202, 58–61. https://doi.org/10.1007/bf00330517 (1986).
doi: 10.1007/bf00330517 pubmed: 3007938
Morfeldt, E., Taylor, D., von Gabain, A. & Arvidson, S. Activation of alpha-toxin translation in Staphylococcus aureus by the trans-encoded antisense RNA RNAIII. EMBO J. 14, 4569–4577 (1995).
doi: 10.1002/j.1460-2075.1995.tb00136.x
Wang, X., Thompson, C. D., Weidenmaier, C. & Lee, J. C. Release of Staphylococcus aureus extracellular vesicles and their application as a vaccine platform. Nat. Commun. 9, 1379. https://doi.org/10.1038/s41467-018-03847-z (2018).
doi: 10.1038/s41467-018-03847-z pubmed: 29643357 pmcid: 5895597
Dastgheyb, S. S. & Otto, M. Staphylococcal adaptation to diverse physiologic niches: an overview of transcriptomic and phenotypic changes in different biological environments. Future Microbiol. 10, 1981–1995. https://doi.org/10.2217/fmb.15.116 (2015).
doi: 10.2217/fmb.15.116 pubmed: 26584249 pmcid: 4946774
Dai, L. et al. Staphylococcus epidermidis recovered from indwelling catheters exhibit enhanced biofilm dispersal and “self-renewal” through downregulation of agr. BMC Microbiol. 12, 102. https://doi.org/10.1186/1471-2180-12-102 (2012).
doi: 10.1186/1471-2180-12-102 pubmed: 22682058 pmcid: 3458918
Cafiso, V. et al. agr-Genotyping and transcriptional analysis of biofilm-producing Staphylococcus aureus. FEMS Immunol. Med. Microbiol. 51, 220–227. https://doi.org/10.1111/j.1574-695X.2007.00298.x (2007).
doi: 10.1111/j.1574-695X.2007.00298.x pubmed: 17854479
Kong, K. F., Vuong, C. & Otto, M. Staphylococcus quorum sensing in biofilm formation and infection. Int. J. Med. Microbiol. IJMM 296, 133–139. https://doi.org/10.1016/j.ijmm.2006.01.042 (2006).
doi: 10.1016/j.ijmm.2006.01.042 pubmed: 16487744
Beenken, K. E. et al. Epistatic relationships between sarA and agr in Staphylococcus aureus biofilm formation. PLoS ONE 5, e10790. https://doi.org/10.1371/journal.pone.0010790 (2010).
doi: 10.1371/journal.pone.0010790 pubmed: 20520723 pmcid: 2875390
Wang, R. et al. Identification of novel cytolytic peptides as key virulence determinants for community-associated MRSA. Nat. Med. 13, 1510–1514. https://doi.org/10.1038/nm1656 (2007).
doi: 10.1038/nm1656 pubmed: 17994102
Periasamy, S. et al. How Staphylococcus aureus biofilms develop their characteristic structure. Proc. Natl. Acad. Sci. USA 109, 1281–1286. https://doi.org/10.1073/pnas.1115006109 (2012).
doi: 10.1073/pnas.1115006109 pubmed: 22232686
Moormeier, D. E. & Bayles, K. W. Staphylococcus aureus biofilm: a complex developmental organism. Mol. Microbiol. 104, 365–376. https://doi.org/10.1111/mmi.13634 (2017).
doi: 10.1111/mmi.13634 pubmed: 28142193 pmcid: 5397344
Foster, T. J., Geoghegan, J. A., Ganesh, V. K. & Hook, M. Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus. Nat. Rev. Microbiol. 12, 49–62. https://doi.org/10.1038/nrmicro3161 (2014).
doi: 10.1038/nrmicro3161 pubmed: 24336184 pmcid: 5708296
Sadykov, M. R. & Bayles, K. W. The control of death and lysis in staphylococcal biofilms: a coordination of physiological signals. Curr. Opin. Microbiol. 15, 211–215. https://doi.org/10.1016/j.mib.2011.12.010 (2012).
doi: 10.1016/j.mib.2011.12.010 pubmed: 22221897 pmcid: 3320683
Diard, M. & Hardt, W. D. Evolution of bacterial virulence. FEMS Microbiol. Rev. 41, 679–697. https://doi.org/10.1093/femsre/fux023 (2017).
doi: 10.1093/femsre/fux023 pubmed: 28531298
Priest, N. K. et al. From genotype to phenotype: can systems biology be used to predict Staphylococcus aureus virulence?. Nat. Rev. Microbiol. 10, 791–797. https://doi.org/10.1038/nrmicro2880 (2012).
doi: 10.1038/nrmicro2880 pubmed: 23070558 pmcid: 7097209
Kahl, B. C., Becker, K. & Loffler, B. Clinical significance and pathogenesis of staphylococcal small colony variants in persistent infections. Clin. Microbiol. Rev. 29, 401–427. https://doi.org/10.1128/cmr.00069-15 (2016).
doi: 10.1128/cmr.00069-15 pubmed: 26960941 pmcid: 4786882
Tuchscherr, L. et al. Clinical S. aureus isolates vary in their virulence to promote adaptation to the host. Toxins (Basel) https://doi.org/10.3390/toxins11030135 (2019).
doi: 10.3390/toxins11030135
Fraunholz, M. & Sinha, B. Intracellular Staphylococcus aureus: live-in and let die. Front. Cell. Infect. Microbiol. 2, 43. https://doi.org/10.3389/fcimb.2012.00043 (2012).
doi: 10.3389/fcimb.2012.00043 pubmed: 22919634 pmcid: 3417557
Cuny, C. et al. Methicillin-resistant Staphylococcus aureus from infections in horses in Germany are frequent colonizers of veterinarians but rare among MRSA from infections in humans. One Health (Amsterdam, Netherlands) 2, 11–17. https://doi.org/10.1016/j.onehlt.2015.11.004 (2016).
doi: 10.1016/j.onehlt.2015.11.004
Golubchik, T. et al. Within-host evolution of Staphylococcus aureus during asymptomatic carriage. PLoS ONE 8, e61319. https://doi.org/10.1371/journal.pone.0061319 (2013).
doi: 10.1371/journal.pone.0061319 pubmed: 23658690 pmcid: 3641031
Skallerup, P., Espinosa-Gongora, C., Jorgensen, C. B., Guardabassi, L. & Fredholm, M. Genome-wide association study reveals a locus for nasal carriage of Staphylococcus aureus in Danish crossbred pigs. BMC Vet. Res. 11, 290. https://doi.org/10.1186/s12917-015-0599-y (2015).
doi: 10.1186/s12917-015-0599-y pubmed: 26612358 pmcid: 4662016
Holtfreter, S. et al. Molecular epidemiology of Staphylococcus aureus in the general population in Northeast Germany: results of the study of health in Pomerania (SHIP-TREND-0). J. Clin. Microbiol. 54, 2774–2785. https://doi.org/10.1128/jcm.00312-16 (2016).
doi: 10.1128/jcm.00312-16 pubmed: 27605711 pmcid: 5078557
Pollitt, E. J., West, S. A., Crusz, S. A., Burton-Chellew, M. N. & Diggle, S. P. Cooperation, quorum sensing, and evolution of virulence in Staphylococcus aureus. Infect. Immun. 82, 1045–1051. https://doi.org/10.1128/iai.01216-13 (2014).
doi: 10.1128/iai.01216-13 pubmed: 24343650 pmcid: 3957977
Paulander, W. et al. Antibiotic-mediated selection of quorum-sensing-negative Staphylococcus aureus. mBio 3, e00459-00412. https://doi.org/10.1128/mBio.00459-12 (2013).
doi: 10.1128/mBio.00459-12
George, S. E. et al. Oxidative stress drives the selection of quorum sensing mutants in the Staphylococcus aureus population. Proc. Natl. Acad. Sci. USA 116, 19145–19154. https://doi.org/10.1073/pnas.1902752116 (2019).
doi: 10.1073/pnas.1902752116 pubmed: 31488708
Schlievert, P. M. et al. Pyrogenic toxin superantigen site specificity in toxic shock syndrome and food poisoning in animals. Infect. Immun. 68, 3630–3634. https://doi.org/10.1128/iai.68.6.3630-3634.2000 (2000).
doi: 10.1128/iai.68.6.3630-3634.2000 pubmed: 10816521 pmcid: 97652
Regassa, L. B. & Betley, M. J. High sodium chloride concentrations inhibit staphylococcal enterotoxin C gene (sec) expression at the level of sec mRNA. Infect. Immun. 61, 1581–1585 (1993).
doi: 10.1128/IAI.61.4.1581-1585.1993
Amissah, N. A. et al. Virulence potential of Staphylococcus aureus isolates from Buruli ulcer patients. Int. J. Med. Microbiol. 307, 223–232. https://doi.org/10.1016/j.ijmm.2017.04.002 (2017).
doi: 10.1016/j.ijmm.2017.04.002 pubmed: 28442219

Auteurs

Charlotte Huber (C)

Advanced Light and Electron Microscopy (ZBS4), Robert Koch Institute, Berlin, Germany.

Ivonne Stamm (I)

IDEXX GmbH, Ludwigsburg, Germany.

Wilma Ziebuhr (W)

Institute for Molecular Infection Biology, University of Würzburg, Würzburg, Germany.

Gabriella Marincola (G)

Institute for Molecular Infection Biology, University of Würzburg, Würzburg, Germany.

Markus Bischoff (M)

Institute of Medical Microbiology and Hygiene, Saarland University, Homburg, Germany.

Birgit Strommenger (B)

National Reference Centre for Staphylococci and Enterococci, Robert Koch Institute, Wernigerode, Germany.

Greta Jaschkowitz (G)

Institute for Molecular Infection Biology, University of Würzburg, Würzburg, Germany.

Tessa Marciniak (T)

Institute for Molecular Infection Biology, University of Würzburg, Würzburg, Germany.

Christiane Cuny (C)

National Reference Centre for Staphylococci and Enterococci, Robert Koch Institute, Wernigerode, Germany.

Wolfgang Witte (W)

National Reference Centre for Staphylococci and Enterococci, Robert Koch Institute, Wernigerode, Germany.

Joerg Doellinger (J)

Proteomics and Spectroscopy (ZBS6), Robert Koch Institute, Berlin, Germany.

Christoph Schaudinn (C)

Advanced Light and Electron Microscopy (ZBS4), Robert Koch Institute, Berlin, Germany.

Andrea Thürmer (A)

Genome Sequencing (MF2), Robert Koch Institute, Berlin, Germany.

Lennard Epping (L)

Microbial Genomics (NG1), Robert Koch Institute, Berlin, Germany.

Torsten Semmler (T)

Microbial Genomics (NG1), Robert Koch Institute, Berlin, Germany.

Antina Lübke-Becker (A)

Institute of Microbiology and Epizootics, Freie Universität Berlin, Berlin, Germany.

Lothar H Wieler (LH)

Methodology and Research Infrastructure, Robert Koch Institute, Berlin, Germany.

Birgit Walther (B)

Advanced Light and Electron Microscopy (ZBS4), Robert Koch Institute, Berlin, Germany. waltherb@rki.de.

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