A point mutation at Asn-534 that disrupts a conserved N-glycosylation motif of the E2 glycoprotein of hepatitis C virus markedly enhances the sensitivity to antibody neutralization.

Title:

A point mutation at Asn-534 that disrupts a conserved N-glycosylation motif of the E2 glycoprotein of hepatitis C virus markedly enhances the sensitivity to antibody neutralization.

Dataset

identifier:	1904348
description:	epitope description:T416 antigen name:Genome polyprotein host organism:Homo sapiens
aggregation:	instance of dataset
availability:	available
primaryPublications:	22170542

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1022701
landingPage:	http://www.iedb.org/assay/1904348

Publication

type:	Literature
publicationVenue:	J Med Virol
dates:	2012

Dimension

study type:	b cell assays
subject species:	Hepatitis C virus JFH-1

Person

fullName:	Mikiko Sasayama Ikuo Shoji Myrna Adianti Da-Peng Jiang Lin Deng Takafumi Saito Hisayoshi Watanabe Sumio Kawata Chie Aoki Hak Hotta

Data Type

method:	biological activity

Study

name:	A point mutation at Asn-534 that disrupts a conserved N-glycosylation motif of the E2 glycoprotein of hepatitis C virus markedly enhances the sensitivity to antibody neutralization.
description:	Recombinant viruses encoding the entire HCV 2a J6/JFH1 genome with point mutation at this residue were rendered sensitive to neutralization by sera from patients infected with acute HCV 1b.

Data Repository

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

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