Functional Mapping of YadA- and Ail-Mediated Binding of Human Factor H to<i>Yersinia enterocolitica</i>Serotype O:3

Biedzka-Sarek, Marta; Salmenlinna, Saara; Gruber, Markus; Lupas, Andrei N.; Meri, Seppo; Skurnik, Mikael

doi:10.1128/iai.00314-08

Cited by 54 publications

(55 citation statements)

References 56 publications

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“…Interestingly, LPS of Y. enterocolitica (LPS YeO3 ), built of distal polysaccharide O-antigen, the core oligosaccharide and the membrane-anchoring lipid A (14 -16), does not protect the bacteria against complement (13). However, outer membrane proteins YadA and Ail, expressed exclusively at 37°C, confer serum resistance via binding of complement regulators (17)(18)(19).…”

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confidence: 99%

Apolipoprotein A-I Exerts Bactericidal Activity against Yersinia enterocolitica Serotype O:3

Biedzka-Sarek

Metso

Kateifides

et al. 2011

Journal of Biological Chemistry

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confidence: 99%

Apolipoprotein A-I Exerts Bactericidal Activity against Yersinia enterocolitica Serotype O:3

Biedzka-Sarek

Metso

Kateifides

et al. 2011

Journal of Biological Chemistry

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“…It is followed by an extended and typically coiled-coil rich stalk, which projects the head from the bacterium and often provides binding sites for host serum factors (10,11). The protein ends in a membrane anchor (2).…”

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confidence: 99%

Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria

Hartmann

Grin

Dunin-Horkawicz

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Trimeric autotransporter adhesins (TAAs) are modular, highly repetitive surface proteins that mediate adhesion to host cells in a broad range of Gram-negative pathogens. Although their sizes may differ by more than one order of magnitude, they all follow the same basic head-stalk-anchor architecture, where the head mediates adhesion and autoagglutination, the stalk projects the head from the bacterial surface, and the anchor provides the export function and attaches the adhesin to the bacterial outer membrane after export is complete. In complex adhesins, head and stalk domains may alternate several times before the anchor is reached. Despite extensive sequence divergence, the structures of TAA domains are highly constrained, due to the tight interleaving of their constituent polypeptide chains. We have therefore taken a "domain dictionary" approach to characterize representatives for each domain type by X-ray crystallography and use these structures to reconstruct complete TAA fibers. With SadA from Salmonella enterica, EhaG from enteropathogenic Escherichia coli (EHEC), and UpaG from uropathogenic E. coli (UPEC), we present three representative structures of a complex adhesin that occur in a conserved genomic context in Enterobacteria and is essential in the infection process of uropathogenic E. coli. Our work proves the applicability of the dictionary approach to understanding the structure of a class of proteins that are otherwise poorly tractable by high-resolution methods and provides a basis for the rapid and detailed annotation of newly identified TAAs.coiled coil | β-layer

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“…It has been shown that factor H, which binds directly to YadA, acts as a cofactor for factor I-mediated degradation of C3b. However, these data also revealed that only a very small amount of C3b present in the experiments was degraded into iC3b (5,20,21). The amount of C3b typically used in these experiments was considerably lower than that of C3 in human serum.…”

Section: Discussionmentioning

confidence: 69%

“…Skurnik and coworkers compared the roles of Yersinia proteins YadA, Ail, and the LPS O-antigen for complement resistance and concluded that YadA is the most potent individual factor mediating resistance against complement-mediated killing. In addition, they demonstrated that surface-bound C3b levels do not correlate with a specific resistance phenotype, but that most strains resistant to complementmediated lysis accumulated iC3b on their surface (20)(21)(22)(23). It was shown that the stalk domain of the YadA trimer is involved in preventing TCC killing (24).…”

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confidence: 99%

“…It was shown that the stalk domain of the YadA trimer is involved in preventing TCC killing (24). As a follow-up, Biedzka-Sarek et al (21) generated a large set of YadA stalk and neck deletion mutants to identify the exact binding domain for factor H. Their data revealed that factor H targets several conformations of YadA and discontinuous sites of the stalk. However, the consequences of deletions in the coiled-coil stalk of YadA are not easily interpreted as distortions of the stalk may influence the structure of distant parts of YadA.…”

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Yersinia enterocolitica YadA Mediates Complement Evasion by Recruitment and Inactivation of C3 Products

Schindler

Schütz

Mühlenkamp

et al. 2012

The Journal of Immunology

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Yersinia adhesin A (YadA) is a major virulence factor of Yersinia enterocolitica. YadA mediates host cell binding and autoaggregation and protects the pathogen from killing by the complement system. Previous studies demonstrated that YadA is the most important single factor mediating serum resistance of Y. enterocolitica, presumably by binding C4b binding protein (C4BP) and factor H, which are both complement inhibitors. Factor H acts as a cofactor for factor I-mediated cleavage of C3b into the inactive form iC3b and thus prevents formation of inflammatory effector compounds and the terminal complement complex. In this study, we challenged the current direct binding model of factor H to YadA and show that Y. enterocolitica YadA recruits C3b and iC3b directly, without the need of an active complement cascade or additional serum factors. Enhanced binding of C3b does not decrease survival of YadA-expressing Yersiniae because C3b becomes readily inactivated by factor H and factor I. Binding of factor H to YadA is greatly reduced in the absence of C3. Experiments using Yersinia lacking YadA or expressing YadA with reduced trimeric stability clearly demonstrate that both the presence and full trimeric stability of YadA are essential for complement resistance. A novel mechanism of factor H binding is presented in which YadA exploits recruitment of C3b or iC3b to attract large amounts of factor H. As a consequence, formation of the terminal complement complex is limited and bacterial survival is enhanced. These findings add a new aspect of how Y. enterocolitica effectively evades the host complement system.

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Functional Mapping of YadA- and Ail-Mediated Binding of Human Factor H toYersinia enterocoliticaSerotype O:3

Cited by 54 publications

References 56 publications

Apolipoprotein A-I Exerts Bactericidal Activity against Yersinia enterocolitica Serotype O:3

Apolipoprotein A-I Exerts Bactericidal Activity against Yersinia enterocolitica Serotype O:3

Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria

Yersinia enterocolitica YadA Mediates Complement Evasion by Recruitment and Inactivation of C3 Products

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