A Vibrio cholerae classical TcpA amino acid sequence induces protective antibody that binds an area hypothesized to be important for toxin-coregulated pilus structure.

Title:

A Vibrio cholerae classical TcpA amino acid sequence induces protective antibody that binds an area hypothesized to be important for toxin-coregulated pilus structure.

Dataset

identifier:	6393
description:	epitope description:GDFENSAAAAETG antigen name:UniProt:A5F392 host organism:Oryctolagus cuniculus New Zealand White
aggregation:	instance of dataset
availability:	available
primaryPublications:	15385509

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/654
landingPage:	http://www.iedb.org/assay/6393

Publication

type:	Literature
publicationVenue:	Infect Immun
dates:	2004

Dimension

study type:	b cell assays
subject species:	Vibrio cholerae O1

Person

fullName:	Ronald K Taylor Thomas J Kirn Michael D Meeks Terri K Wade William F Wade

Data Type

method:	western blot

Study

name:	A Vibrio cholerae classical TcpA amino acid sequence induces protective antibody that binds an area hypothesized to be important for toxin-coregulated pilus structure.
description:	In additional Western Blot assays, it was shown that anti-TcpA polypeptide sera did not react strongly with folded, soluble TcpA subunits, which were genetically substituted and grown in E. coli to enhance formation of the TcpA disulfide bond.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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