The immunoglobulin-binding Eib proteins from Escherichia coli are receptors for IgG Fc

Leo, Jack C.; Goldman, Adrian

doi:10.1016/j.molimm.2009.02.024

Cited by 38 publications

(35 citation statements)

References 14 publications

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“…Finally, we tested whether the heterotrimers are able to bind IgG Fc nonimmunologically (23). We performed standard Western blotting with Fc(IgG)-HRP and developed the blot with the substrate for HRP (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…This finding is very interesting as multiple Eib genes occur naturally in E. coli strains (37). Their natural coexpression can result in the binding of different subsets of Igs as different Eibs bind with various affinities or not at all to different Ig subtypes (23,37,38). There are two possibilities: either bacteria have a mechanism that prevents heterotrimerization, or heterotrimers form and are at least not disadvantageous.…”

Section: Discussionmentioning

confidence: 99%

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The Translocation Domain in Trimeric Autotransporter Adhesins Is Necessary and Sufficient for Trimerization and Autotransportation

et al. 2012

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Trimeric autotransporter adhesins (TAAs) comprise one of the secretion pathways of the type V secretion system. The mechanism of their translocation across the outer membrane remains unclear, but it most probably occurs by the formation of a hairpin inside the ␤-barrel translocation unit, leading to transportation of the passenger domain from the C terminus to the N terminus through the lumen of the ␤-barrel. We further investigated the phenomenon of autotransportation and the rules that govern it. We showed by coexpressing different Escherichia coli immunoglobulin-binding (Eib) proteins that highly similar TAAs could form stochastically mixed structures (heterotrimers). We further investigated this phenomenon by coexpressing two more distantly related TAAs, EibA and YadA. These, however, did not form heterotrimers; indeed, coexpression was lethal to the cells, leading to elimination of one or another of the genes. However, substituting in either protein the barrel of the other one so that the barrels were identical led to formation of heterotrimers as for Eibs. Our work shows that trimerization of the ␤-barrel, but not the passenger domain, is necessary and sufficient for TAA secretion while the passenger domain is not.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The Translocation Domain in Trimeric Autotransporter Adhesins Is Necessary and Sufficient for Trimerization and Autotransportation

et al. 2012

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“…(42)(43)(44)(45)(46). This group of bacterial Fc binding proteins also includes the E. coli immunoglobulin binding (Eib) proteins, consisting of six homologous proteins (EibA, -C, -D, -E, -F and -G), which have been shown to increase resistance of the bacteria to human serum complement system (47,48). In regard to the potential function of InvD in the context of antibody-binding, we can exclude a function as phagocytosis inhibitor or complement resistance factor, as seen for SpA, Sbi or Eib (function I. described above), because InvD clearly binds to the Fab but not to the Fc part.…”

Section: Discussionmentioning

confidence: 99%

The invasin D protein from Yersinia pseudotuberculosis selectively binds the Fab region of host antibodies and affects colonization of the intestine

Sadana

Geyer

Pezoldt

et al. 2018

Journal of Biological Chemistry

576

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“…In the case of the STEC O91 EibG, it was found that this protein has dual roles: it binds human IgG and IgA and also participates in bacterial adherence to host epithelial cells (51). A recent study further evaluated whether Eib proteins bind to the Fc portion of IgG in a nonimmune manner and concluded that these proteins do indeed bind human IgG Fc and that IgG Fc receptors are present in E. coli strains (48). Finally, the prevalence of the eibG gene and its allelic variations, as well as their correlation with the CLA phenotype, was evaluated with a large collection of STEC strains (56).…”

Section: Other Stec Adhesinsmentioning

confidence: 99%

Molecular Mechanisms That Mediate Colonization of Shiga Toxin-Producing Escherichia coli Strains

2012

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Shiga toxin-producing Escherichia coli (STEC) is a group of pathogens which cause gastrointestinal disease in humans and have been associated with numerous food-borne outbreaks worldwide. The intimin adhesin has been considered for many years to be the only colonization factor in these strains. However, the rapid progress in whole-genome sequencing of different STEC serotypes has accelerated the discovery of other adhesins (fimbrial and afimbrial), which have emerged as important contributors to the intestinal colonization occurring during STEC infection. This review summarizes recent progress to identify and characterize, at the molecular level, novel adhesion and colonization factors in STEC strains, with an emphasis on their contribution to virulence traits, their host-pathogen interactions, the regulatory mechanisms controlling their expression, and their role as targets eliciting immune responses in the host. STEC O157:H7 AND NON-O157 STEC Shiga-toxigenic Escherichia coli (STEC) O157:H7 is an important cause of human gastrointestinal disease and the beststudied STEC associated with large outbreaks worldwide (43, 74). STEC O157:H7 strains cause diarrhea, hemorrhagic colitis, and hemolytic uremic syndrome (HUS) (59). Disease-associated human isolates of E. coli O157:H7 are characterized for the presence of specific sets of virulence genes, including those encoding Shigatoxins (stx 1 , stx 2 ), intimin (eae), hemolysin (hlyA), and long polar fimbriae (lpf1 and lpf2) (45, 97). The production of Stx is the main virulence feature of STEC associated with the development of HUS (82) but cannot be solely responsible for full pathogenicity. STEC associated with severe human disease is usually capable of colonizing the intestinal mucosa and possesses mobile genetic elements carrying virulence genes, such as plasmids, transposons, phages, and pathogenicity islands (79,92,97). Several important colonization properties are carried by the locus of enterocyte effacement (LEE) pathogenicity island (92), which governs the ability of STEC to colonize the intestinal mucosa of the host and produces a peculiar pathogenic process known as the attachingand-effacing (A/E) lesion (for a review, see reference 59).Most virulence/colonization factors have been described for STEC O157:H7 isolates; however, it is important to identify and determine the virulence traits of other STECs important for disease in humans, the so-called "non-O157 STEC" strains. In addition to diarrhea, these isolates are also associated with severe disease. Several serogroups of non-O157 STEC have been described; however, the serogroups O26, O45, O103, O111, and O145 have been identified as the "big six" non-O157 STEC O serogroups, because they have been associated with increasing frequency in patients with bloody diarrhea and HUS (12,29,41,55). Because the U.S. Food and Drug Administration recognizes that non-O157 STEC serogroups are emerging as an important cause of food-borne disease, these isolates impact both the imported and domestic food supply. Therefor...

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The immunoglobulin-binding Eib proteins from Escherichia coli are receptors for IgG Fc

Cited by 38 publications

References 14 publications

The Translocation Domain in Trimeric Autotransporter Adhesins Is Necessary and Sufficient for Trimerization and Autotransportation

The Translocation Domain in Trimeric Autotransporter Adhesins Is Necessary and Sufficient for Trimerization and Autotransportation

The invasin D protein from Yersinia pseudotuberculosis selectively binds the Fab region of host antibodies and affects colonization of the intestine

Molecular Mechanisms That Mediate Colonization of Shiga Toxin-Producing Escherichia coli Strains

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