Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/516 |
| landingPage: |
http://www.iedb.org/assay/8561 |
| type: |
Literature
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| publicationVenue: |
J Struct Biol
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| dates: |
2004
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| study type: | b cell assays |
| subject species: | Salmonella enterica subsp. enterica serovar Typhi |
| fullName: |
A Arockiasamy
G S Murthy
M R Rukmini
N Sundara Baalaji
Umesh Chandra Katpally
S Krishnaswamy
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| method: |
western blot
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| name: |
Conformational epitope mapping of OmpC, a major cell surface antigen from Salmonella typhi.
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| description: |
The amino acids shown in the Conformational Sequence field are the key residues for the binding of monoclonal antibodies to the outer membrane protein (OmpC). These key residues were identified using antibodies, chemical modification and solid phase binding methods. The antibody that binds to this epitope is enterobacterial porin-specific but also binds to Salmonella typhi. (The epitope source listed is the precursor protein --- the amino acid positions given refer to the mature protein.)"""" The porin OmpC from Salmonella typhi is a 16-stranded porin. The possible expression of OmpC throughout the infection period and its capacity to display heterologous epitopes on the cell surface make it an important candidate antigen with potential applications in immunology and vaccine design.S. typhi OmpC, outer membrane protein, is a homotrimer with 357 amino acids and MW 39 kDa/monomer and has large loops.
The dot blot with whole cell and the extracted porin indicated that the epitopes are formed by the surface exposed loops of the porin trimer. The recognition of porin in the whole cell blot by the MAbs (P7D8) indicated that the epitopes are surface exposed and formed by the loops. The P7D8 monoclonal antibody binds to the trimeric structure of the porin, but not the monomeric form.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
