Binding of extracellular matrix laminin to Escherichia coli expressing the Salmonella outer membrane proteins Rck and PagC

Crago, Aimeé M.

doi:10.1016/s0378-1097(99)00279-7

Cited by 20 publications

(20 citation statements)

References 11 publications

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“…However, as the molecular mechanisms of these proteins become characterized, it is apparent that conserved functions can be assigned to several members of this family. Rck, PagC (Salmonella choleraesuis), and Ail were shown to mediate serum resistance (3-5, 23, 24), whereas adhesion and/or invasion properties have been observed in all of the aforementioned proteins, with the exception of Y. pseudotuberculosis Ail (25)(26)(27)(28)(29). Furthermore, functional fH and C4BP binding have now been described in Rck (21,30) and Y. enterocolitica and Y. pseudotuberculosis Ail (10,11,15).…”

Section: Discussionmentioning

confidence: 99%

The Yersinia pseudotuberculosis Outer Membrane Protein Ail Recruits the Human Complement Regulatory Protein Factor H

Riva

Skurnik

et al. 2012

The Journal of Immunology

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Previous investigations characterizing the mechanism(s) of complement resistance in Yersinia pseudotuberculosis showed that the outer membrane protein Ail can functionally recruit the regulator of the classical and lectin pathways of complement, C4b-binding protein. In this study, we extend these observations and show that Ail can also recruit the regulator of the alternative pathway (AP), factor H (fH). Binding to fH was dependent on Ail expression and observed in the context of full-length LPS. Inactivation of ail resulted in loss of fH binding. Ail expression conferred resistance to AP-mediated killing. Bound fH was functional as a cofactor for factor I-mediated cleavage and inactivation of C3b. Ail alone is sufficient to mediate fH binding and resistance to AP-mediated killing, because Ail expression in a laboratory Escherichia coli strain conferred both of these phenotypes. Binding was specific and inhibited by increasing heparin and NaCl concentrations. Using a panel of fH recombinant fragments, we observed that both short consensus repeats 5–7 and 19–20 regions are responsible for mediating the interaction with Ail. Collectively, these results suggest that fH recruitment is an additional mechanism of complement resistance of Ail. Recruitment of both fH and C4BP by Ail may confer Y. pseudotuberculosis with the ability to resist all pathways of complement activation.

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Section: Discussionmentioning

confidence: 99%

The Yersinia pseudotuberculosis Outer Membrane Protein Ail Recruits the Human Complement Regulatory Protein Factor H

Riva

Skurnik

et al. 2012

The Journal of Immunology

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“…The Salmonella protein Rck was first identified as a virulence factor required for serum resistance and host cell invasion (9). It was later found that both Rck and a similar protein, PagC, are able to bind laminin, and their expression in Escherichia coli confers the capacity for adherence to basement membranes and host cells (11). Adherence to ECM is also believed to contribute to virulence of Bacteroides fragilis, Borrelia burgdorferi, Haemophilus influenzae, and Moraxella catarrhalis (6,18,19,53).…”

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confidence: 99%

Helicobacter pylori AlpA and AlpB Bind Host Laminin and Influence Gastric Inflammation in Gerbils

et al. 2011

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Helicobacter pylori persistently colonizes humans, causing gastritis, ulcers, and gastric cancer. Adherence to the gastric epithelium has been shown to enhance inflammation, yet only a few H. pylori adhesins have been paired with targets in host tissue. The alpAB locus has been reported to encode adhesins involved in adherence to human gastric tissue. We report that abrogation of H. pylori AlpA and AlpB reduces binding of H. pylori to laminin while expression of plasmid-borne alpA or alpB confers laminin-binding ability to Escherichia coli. An H. pylori strain lacking only AlpB is also deficient in laminin binding. Thus, we conclude that both AlpA and AlpB contribute to H. pylori laminin binding. Contrary to expectations, the H. pylori SS1 mutant deficient in AlpA and AlpB causes more severe inflammation than the isogenic wild-type strain in gerbils. Identification of laminin as the target of AlpA and AlpB will facilitate future investigations of host-pathogen interactions occurring during H. pylori infection.

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“…Heffernan and coworkers (10) have demonstrated that Rck appears to affect the formation and interaction of the MAC on the bacterial surface, as Rck-expressing cells are more sensitive to trypsin release of C9 and display fewer SDS-resistant C5b-9 complexes, suggesting disruption of MAC function (8). In addition to serum resistance, Rck expression in E. coli mediates adherence and invasion to cultured eukaryotic cell lines (10) as well as binding to laminin and fibronectin (11).…”

mentioning

confidence: 99%

Human Complement Factor H Binds to Outer Membrane Protein Rck of Salmonella

Jarva

Meri

2010

The Journal of Immunology

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Serum resistance, or resistance to complement-mediated killing, is a key virulence property of microbial pathogens. Rck is a 17-kDa outer membrane protein encoded on the virulence plasmid of Salmonella enterica serovars Typhimurium and Enteritidis. When expressed in either Escherichia coli or S. enterica Typhimurium, Rck confers serum resistance independent of LPS length. Recently, the Rck homolog from Yersinia enterocolitica, Ail, has been shown to bind the complement regulatory protein factor H (fH). Based on these observations, we hypothesized that Rck may also possess this ability. Using both flow cytometery and direct binding analysis, we demonstrate that Rck expressed in E. coli binds fH. We observed fH binding to Rck from human serum and also using the purified protein. Expression of Rck protected bacteria from alternative pathway-mediated killing and was associated with a reduction in C3b, Bb, and membrane attack complex deposition. fH bound to Rck promoted C3b cleavage in the presence of factor I. Binding was specific and mediated by two regions in fH, the short consensus repeats 5–7 and 19 to 20. These results suggest that fH recruitment by Rck is functional and can protect a normally serum-sensitive heterologous host against complement attack. Binding and exploitation of fH may thus contribute to Rck-mediated serum resistance.

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Binding of extracellular matrix laminin to Escherichia coli expressing the Salmonella outer membrane proteins Rck and PagC

Cited by 20 publications

References 11 publications

The Yersinia pseudotuberculosis Outer Membrane Protein Ail Recruits the Human Complement Regulatory Protein Factor H

The Yersinia pseudotuberculosis Outer Membrane Protein Ail Recruits the Human Complement Regulatory Protein Factor H

Helicobacter pylori AlpA and AlpB Bind Host Laminin and Influence Gastric Inflammation in Gerbils

Human Complement Factor H Binds to Outer Membrane Protein Rck of Salmonella

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