Blom, Anna,

Ho, Derek K.

Jarva, Hanna

Jarvinen, Hanna M.

Lund University.

Meri, Seppo

Tissari, Jorma

PLoS ONE

PubMed

Resistance to complement mediated killing, or serum resistance, is a common trait of pathogenic bacteria. Rck is a 17 kDa outer membrane protein encoded on the virulence plasmid of Salmonella enterica serovars Typhimurium and Enteritidis. When expressed in either E. coli or S. enterica Typhimurium, Rck confers LPS-independent serum resistance as well as the ability to bind to and invade mammalian cells. Having recently shown that Rck binds the inhibitor of the alternative pathway of complement, factor H (fH), we hypothesized that Rck can also bind the inhibitor of the classical and lectin pathways, C4b-binding protein (C4BP). Using flow cytometry and direct binding assays, we demonstrate that E. coli expressing Rck binds C4BP from heat-inactivated serum and by using the purified protein. No binding was detected in the absence of Rck expression. C4BP bound to Rck is functional, as we observed factor I-mediated cleavage of C4b in cofactor assays. In competition assays, binding of radiolabeled C4BP to Rck was reduced by increasing concentrations of unlabeled protein. No effect was observed by increasing heparin or salt concentrations, suggesting mainly non-ionic interactions. Reduced binding of C4BP mutants lacking complement control protein domains (CCPs) 7 or 8 was observed compared to wt C4BP, suggesting that these CCPs are involved in Rck binding. While these findings are restricted to Rck expression in E. coli, these data suggest that C4BP binding may be an additional mechanism of Rck-mediated complement resistance

Blom, Anna

Lund University Publications

English

Functional Recruitment of Human Complement Inhibitor C4b-Binding Protein to Outer Membrane Protein Rck of Salmonella

Blom, Anna M.

Helsingin yliopiston digitaalinen arkisto

Swepub

Functional Recruitment of Human Complement Inhibitor C4b-Binding Protein to Outer Membrane Protein Rck of Salmonella [Elektronisk resurs]

Derek K Ho

Jorma Tissari

Hanna M Järvinen

Anna M Blom

Seppo Meri

Hanna Jarva

Directory of Open Access Journals

Functional recruitment of human complement inhibitor C4B-binding protein to outer membrane protein Rck of Salmonella.

Derek K. Ho

Hanna M. Järvinen

Anna M. Blom

Crossref

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Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica.

Structural and functional studies of complement inhibitor C4bbinding protein.

Structural requirements for the complement regulatory activities of C4BP.

Studies on the mechanism of bacterial resistance to complement-mediated killing. I. Terminal complement components are deposited and released from Salmonella minnesota S218 without causing bacterial death.

The Salmonella typhimurium virulence plasmid complement resistance gene rck is homologous to a family of virulence-related outer membrane protein genes, including pagC and ail.

The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence.

The surface protease PgtE of Salmonella enterica affects complement activity by proteolytically cleaving C3b, C4b and C5.

Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein.

http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3213152

Functional Recruitment of Human Complement Inhibitor C4b-Binding Protein to Outer Membrane Protein Rck of Salmonella

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Lund University Publications

Helsingin yliopiston digitaalinen arkisto

Swepub

Directory of Open Access Journals

Crossref