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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-6-2
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pubmed:abstractText |
The Salmonella typhi (St) ompC gene codes for a major outer membrane protein (OMP) that is highly expressed in both low and high osmolarity. By hybridization studies with the entire gene or with segments thereof, ompC was found to be highly conserved within 11 different Salmonella serotypes, with the exception of S. arizonae. The study included several St isolates from Mexico and Indonesia. Variation was only detected in two (e and f) of the seven regions previously found to vary between St and E. coli ompC. Chimeric OmpC proteins, carrying a rotavirus VP4 capsid protein epitope, are well recognized by a specific monoclonal antibody (mAb) against this epitope, either in OMP preparations (by enzyme-linked immunosorbent assay; ELISA) or intact cells (by ELISA and immunogold-labelling), indicating that regions c and f are oriented towards the cell surface and are probably exposed. As has been shown before for other regulated OMP, this experimental approach could be useful for the presentation of heterologous epitopes in order to gain knowledge about porin topology, for testing the effect of altered porin surface epitopes on bacterial physiology, or else, in the development of multivalent vaccines.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VP4 protein, Rotavirus
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0378-1119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
156
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pubmed:geneSymbol |
ompC
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7537703-Amino Acid Sequence,
pubmed-meshheading:7537703-Bacterial Outer Membrane Proteins,
pubmed-meshheading:7537703-Base Sequence,
pubmed-meshheading:7537703-Capsid,
pubmed-meshheading:7537703-Capsid Proteins,
pubmed-meshheading:7537703-Conserved Sequence,
pubmed-meshheading:7537703-Epitopes,
pubmed-meshheading:7537703-Genes, Bacterial,
pubmed-meshheading:7537703-Genetic Variation,
pubmed-meshheading:7537703-Genotype,
pubmed-meshheading:7537703-Molecular Sequence Data,
pubmed-meshheading:7537703-Polymorphism, Restriction Fragment Length,
pubmed-meshheading:7537703-Protein Conformation,
pubmed-meshheading:7537703-Recombinant Fusion Proteins,
pubmed-meshheading:7537703-Rotavirus,
pubmed-meshheading:7537703-Salmonella,
pubmed-meshheading:7537703-Salmonella typhi
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pubmed:year |
1995
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pubmed:articleTitle |
The Salmonella ompC gene: structure and use as a carrier for heterologous sequences.
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pubmed:affiliation |
Departamento de Microbiología Molecular, Universidad Nacional Autónoma de México, Cuernavaca.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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