Immunological cross-reactivity between outer membrane pore proteins of Campylobacter jejuni and Escherichia coli

Kervella, Michèle

doi:10.1016/0378-1097(92)90041-l

Cited by 9 publications

(13 citation statements)

References 8 publications

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“…It is known that the size (ranging from 40 to 48 kDa as estimated by denaturing SDS-PAGE) and antigenicity of MOMP may vary in different strains of C. jejuni (5,6,19). However, the genetic basis for MOMP heterogeneity has not been determined.…”

Section: Resultsmentioning

confidence: 99%

Sequence Polymorphism, Predicted Secondary Structures, and Surface-Exposed Conformational Epitopes of Campylobacter Major Outer Membrane Protein

et al. 2000

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The major outer membrane protein (MOMP), a putative porin and a multifunction surface protein of Campylobacter jejuni, may play an important role in the adaptation of the organism to various host environments. To begin to dissect the biological functions and antigenic features of this protein, the gene (designated cmp) encoding MOMP was identified and characterized from 22 strains of C. jejuni and one strain of C. coli. It was shown that the single-copy cmp locus encoded a protein with characteristics of bacterial outer membrane proteins. Prediction from deduced amino acid sequences suggested that each MOMP subunit consisted of 18 ␤-strands connected by short periplasmic turns and long irregular external loops. Alignment of the amino acid sequences of MOMP from different strains indicated that there were seven localized variable regions dispersed among highly conserved sequences. The variable regions were located in the putative external loop structures, while the predicted ␤-strands were formed by conserved sequences. The sequence homology of cmp appeared to reflect the phylogenetic proximity of C. jejuni strains, since strains with identical cmp sequences had indistinguishable or closely related macrorestriction fragment patterns. Using recombinant MOMP and antibodies recognizing linear or conformational epitopes of the protein, it was demonstrated that the surface-exposed epitopes of MOMP were predominantly conformational in nature. These findings are instrumental in the design of MOMP-based diagnostic tools and vaccines.

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Section: Resultsmentioning

confidence: 99%

Sequence Polymorphism, Predicted Secondary Structures, and Surface-Exposed Conformational Epitopes of Campylobacter Major Outer Membrane Protein

et al. 2000

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“…The MOMP and E. coli OmpC common antigenic site. Antigenic cross-reactivity between the MOMP and E. coli porins had previously been investigated, and interestingly, only the OmpC porin was recognized by an antiserum specific to the MOMP (22). To characterize the conserved antigenic region between the MOMP and OmpC, various chimeric porins (12,17) containing different OmpC domains were used (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…C. jejuni 85H was obtained from M. Kervella (22). Cells were grown on Columbia agar medium under microaerobic conditions at 42ЊC for 48 h.…”

Section: Methodsmentioning

confidence: 99%

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Conformational analysis of the Campylobacter jejuni porin

et al. 1995

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The major outer membrane protein (MOMP) of Campylobacter jejuni was purified to homogeneity by selective solubilization and fast protein liquid chromatography. The amino acid composition of the MOMP indicates the presence of cysteine residues. The amino-terminal sequence, determined over 31 residues, shows no significant homology with any other porin from gram-negative bacteria except in a discrete region. Immunocross-reactivity between Escherichia coli OmpC and the MOMP was analyzed, and a common antigenic site between these two porins was identified with an anti-peptide antibody. From circular dichroism and immunological investigations, the existence of a stable folded monomer, containing a high level of ␤-sheet secondary structure, is evident. Conformational analyses show the presence of a native trimeric state generated by association of the three folded monomers; the stability of this trimer is reduced compared with that of E. coli porins. This study clearly reveals that the C. jejuni MOMP is related to the family of trimeric bacterial porins.The gram-negative bacterium Campylobacter jejuni is responsible for enteritis and diarrhea all over the world, in both industrialized and developing countries (41). Since 1970, this bacterium and other Campylobacter species have been routinely isolated from stools and other specimens. Numerous studies that have tried to elucidate the molecular mechanisms of pathogenicity have been done in several laboratories. Flagella play a role in mobility in the luminal mucosa, which appears to be one of the most important steps in the colonization of the host gut (14,15,33). Moreover, little is known about the structural and functional organization of the bacterial envelope.Porins of gram-negative bacteria are involved in the diffusion of solutes through this envelope and are the most common way of communication between bacteria and media (16,34). In Escherichia coli, the major outer membrane porins, OmpF and OmpC, have different pore sizes and their synthesis depends on external conditions (36). A previous report has established that the major outer membrane protein (MOMP) of C. jejuni presents the physicochemical properties of a porin (18). Although the stabilities of porin trimers are a peculiarity of these membrane pore proteins (32, 38), there are some divergent views on the quaternary structure of this MOMP (1,18,27). Recent studies of E. coli OmpA have reported a pore activity for this monomeric protein previously described as an architectural component of the bacterial envelope (36, 40). Similarly, a monomeric porin, showing noticeable homology with the OmpA sequence, was also isolated from Pseudomonas aeroginosa (2, 7). In addition, the electrophoretic migrations of these proteins are similarly modified by the temperature of solubilization (6,7,18). These results suggest that monomeric OmpA-like proteins form channels in the outer membranes of gram-negative bacteria (35).The purification and determination of the amino acid composition and amino-terminal sequence of the MO...

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“…Previous reports showed that antibodies to outer-membrane proteins (OMPs) were protective in experimentally induced infection in mice [16][17][18][19][20][21]. Other authors found anti-OMP antibodies that cross-reacted with protein epitopes of different gram-negative serotypes [7,24,25]. Furthermore, Hofstra et al showed crossreactivity among OMPs of members of the Enterobacteriaceae in crossed immuno-electrophoretic studies [26], and recent studies [14] showed that an antiserum raised to E. coli J5 contained high titres of IgG antibodies that bound to at least three major OMPs on many clinically relevant gram-negative bacteria.…”

Section: Discussionmentioning

confidence: 99%

Protective features of monoclonal antibodies to Escherichia coli during experimental infection of mice with homologous and heterologous serotypes of E. coli

Raponi¹,

Ghezzi²,

Lun³

et al. 2000

Journal of Medical Microbiology

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Murine monoclonal antibodies (MAbs) MT1F and ARM1-4, recognising proteins on the surface of untreated Escherichia coli O6:K 2 , protected 100% of mice challenged intraperitoneally with 2 3 LD50 of the same strain. MAb MT1F protected 70% of animals challenged with 2 3 LD50 of E. coli O111:B4, whereas ARM1-4 gave complete protection. Lower survival was observed in mice given either MAb and challenged with E. coli O128:K 2 , with values ranging from 30 to 42%. However, the protection afforded against E. coli O111:B4 and E. coli O128:K 2 was significantly improved when the mice were pre-treated with a mixture of the two MAbs. Control mice, pre-treated with unrelated ascitic fluid and challenged with any of the E. coli serotypes, showed 100% mortality and organ histological lesions resembling those of the early stages of septic shock. The mice had high levels of circulating endotoxin and tumour necrosis factor-AE (TNF-AE) at 90 min after challenge. In contrast, mice treated with MAbs and surviving the infection displayed moderate histological lesions, enhanced bacterial clearance and lower serum levels of TNF-AE, despite circulating endotoxin levels that were higher than in the control group. Protection by the MAbs was probably due to the prevention of the bacterial spread to organs and of the cascade of events leading to septic shock. This occurred in spite of the presence of high levels of circulating endotoxin.

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Immunological cross-reactivity between outer membrane pore proteins of Campylobacter jejuni and Escherichia coli

Cited by 9 publications

References 8 publications

Sequence Polymorphism, Predicted Secondary Structures, and Surface-Exposed Conformational Epitopes of Campylobacter Major Outer Membrane Protein

Sequence Polymorphism, Predicted Secondary Structures, and Surface-Exposed Conformational Epitopes of Campylobacter Major Outer Membrane Protein

Conformational analysis of the Campylobacter jejuni porin

Protective features of monoclonal antibodies to Escherichia coli during experimental infection of mice with homologous and heterologous serotypes of E. coli

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