Immunological approach of assembly and topology of OmpF, an outer membrane protein of Escherichia coli

Pages, J.-M.; Bolla, Jean‐Michel; Bernadac, Alain; Fourel, Didier

doi:10.1016/0300-9084(90)90142-4

Cited by 12 publications

(5 citation statements)

References 63 publications

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“…Eight of these were raised against trimers, and among these, six MAbs reacted only with the immunogen (homologous) trimer, whether purified or as a component of OM or whole cells. These results, in agreement with previous studies (9,24,45,57), identify antibodies that bind surface epitopes of the trimers. These determinants are presumably conformational rather than sequential, because they are not recognized if the trimers are denatured to monomers.…”

Section: Methodssupporting

confidence: 93%

“…The six antibodies that bind only homologous trimer (Table 1) demonstrate that sequence variability exists in the cell-surface-exposed parts of the three related Salmonella pore proteins. This is consistent with findings of several other studies which have shown that MAbs directed against native porins fail to detect common antigenic sites among, PhoE, OmpC, and OmpF pore proteins (2,45,57,61), despite high sequence homology and cross-reactivity with polyclonal antisera (43). Since surface domains of OM proteins act as receptors for phages and colicins, the variability in their constituent residues may arise from selective pressure to evade such toxic agents and antibodies (4).…”

Section: Methodssupporting

confidence: 90%

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Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC

et al. 1992

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The immunochemistry and structure of enteric bacterial porins are critical to the understanding of the immune response to bacterial infection. We raised 41 monoclonal antibodies (MAbs) to SalmoneUla typhimurium OmpD and OmpC porin trimers and monomers. Enzyme-linked immunosorbent assays, immunoprecipitations, and/or Western immunoblot techniques indicated that 39 in the panel are porin specific and one binds to the lipopolysaccharide; the specificity of the remaining MAb probably lies in the porin-lipopolysaccharide complex. Among the porin-specific MAbs, 10 bound cellsurface-exposed epitopes, one reacted with a periplasmic epitope, and the remaining 28 recognized determinants that are buried within the outer membrane bilayer. Many of the MAbs reacting with surface-exposed epitopes were highly specific, recognizing only the homologous porin trimers; this suggests that the cellsurface-exposed regions of porins tend to be quite different among S. typhimurium OmpF, OmpC, and OmpD porins. Immunological cross-reaction showed that S. typhimurium OmpD was very closely related to Escherichia coli NmpC and to the Lc porin of bacteriophage PA-2. Immunologically, E. coli OmpG and protein K also appear to belong to the family of closely related porins including E. coli OmpF, OmpC, PhoE, and NmpC and S. typhimurium OmpF, OmpC, and OmpD. It appears, however, that S. typhimurium "PhoE" is not closely related to this group. Finally, about one-third of the MAbs that presumably recognize buried epitopes reacted with porin domains that are widely conserved in 13 species of the family Enterobacteriaceae, but apparently not in the seven nonenterobacterial species tested. These data are evaluated in relation to host immune response to infection by gram-negative bacteria.

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Section: Methodssupporting

confidence: 93%

Section: Methodssupporting

confidence: 90%

Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC

et al. 1992

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“…Boyd and Holland, 1980; Freudl et al ., 1986), but with the exception of the novel extended α‐β‐barrel protein TolC (Werner et al ., 2003), no definitive experiments have yet demonstrated that these OMPs are true intermediates and not the result of off‐pathway by‐products that were unable to properly assemble. Further confounding the issue is that different OMPs have been shown both in vivo and in vitro to have differential requirements for LPS (Bolla et al ., 1988; Pages et al ., 1990; Ried et al ., 1990), phospholipids (Surrey and Jähnig, 1995; Kloser et al ., 1998) and periplasmic chaperones and/or folding factors for proper OMP assembly (Mogensen and Otzen, 2005 and references therein). An alternative to the periplasmic transport route model is that OMPs bypass the periplasm passing through proteinaceous fusion sites (Smit and Nikaido, 1978), as appears to be the case for LPS.…”

Section: Introductionmentioning

confidence: 99%

YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli

Malinverni

Werner

Kim

et al. 2006

Molecular Microbiology

285

376

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“…Resistance to the action of the membrane attack complex is often observed when bacteria change from a rough to a smooth phenotype. LPS of gram-negative bacteria are closely associated with the major OMPs (porins) (25,30). It is probable that the length of the LPS chains determines the accessibility of complement to bacterial components such as porins and that effectiveness of complement fixation is also related to the nature of the LPS sugars.…”

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confidence: 99%

Role of Virulence Factors in Resistance of Avian Pathogenic Escherichia coli to Serum and in Pathogenicity

et al. 2003

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In chickens, colibacillosis is caused by avian pathogenic Escherichia coli (APEC) via respiratory tract infection. Many virulence factors, including type 1 (F1A) and P (F11) fimbriae, curli, aerobactin, K1 capsule, and temperature-sensitive hemagglutinin (Tsh) and plasmid DNA regions have been associated with APEC. A strong correlation between serum resistance and virulence has been demonstrated, but roles of virulence factors in serum resistance have not been well elucidated. By using mutants of APEC strains TK3, MT78, and 7122, which belong to serogroups O1, O2, and O78, respectively, we investigated the role of virulence factors in resistance to serum and pathogenicity in chickens. Our results showed that serum resistance is one of the pathogenicity mechanisms of APEC strains. Virulence factors that increased bacterial resistance to serum and colonization of internal organs of infected chickens were O78 lipopolysaccharide of E. coli 7122 and the K1 capsule of E. coli MT78. In contrast, curli, type 1, and P fimbriae did not appear to contribute to serum resistance. We also showed that the iss gene, which was previously demonstrated to increase resistance to serum in certain E. coli strains, is located on plasmid pAPEC-1 of E. coli 7122 but does not play a major role in resistance to serum for strain 7122.Avian pathogenic Escherichia coli (APEC) belongs to the extraintestinal pathogenic group of E. coli. These bacteria cause airsacculitis, omphalitis, peritonitis, salpingitis, synovitis, and colisepticemia in poultry (17). APEC is also associated with cellulitis or necrotic dermatitis of the lower abdomen and thighs and with granuloma. APEC strains belong predominantly to three serogroups, O1, O2, and O78. Virulence factors associated with APEC strains include type 1 and P fimbriae, curli, aerobactin, K1 capsule, and temperature-sensitive hemagglutinin (Tsh) of the autotransporter family (9, 17). Serum resistance also appears to be an important virulence mechanism of APEC, and it may play a major role in the pathogenesis of avian colibacillosis. For instance, serum resistance has often been associated with isolates from septicemic turkeys and chickens (13,33), and a correlation between serum resistance and virulence and lethality in isolates from septicemic chickens and turkeys has been observed (13,15,17).At this time, it is not known if avian E. coli strains differ from mammalian isolates in their mechanisms of serum resistance and virulence. Studies carried out with mammalian E. coli showed that many virulence factors, such as capsules, lipopolysaccharide (LPS), and outer membrane proteins (OMPs), includingOmpA and the ColV plasmid-encoded proteins TraT and Iss, are associated with complement resistance of E. coli (17). TraT is a surface exclusion protein encoded by conjugative plasmids (32), and Iss is a plasmid-encoded OMP homologous to the Bor protein of bacteriophage (32). In APEC, the role of different virulence factors in serum resistance has generally been speculative. Nolan et al. (22) produced an a...

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Immunological approach of assembly and topology of OmpF, an outer membrane protein of Escherichia coli

Cited by 12 publications

References 63 publications

Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC

Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC

YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli

Role of Virulence Factors in Resistance of Avian Pathogenic Escherichia coli to Serum and in Pathogenicity

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