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identifier: 2019390
description:
epitope description:I422, T425, L427, N428, C429, N430, E431, S432, L433, N434, G436, L438, A439, L441, F442, Y443, Q444, H445, K446, P505, S528, W529, A531, Y613
antigen name:Genome polyprotein
host organism:Homo sapiens
antibody name:AR3C
aggregation:
instance of dataset
availability:
available
primaryPublications: 24288331
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1027028
landingPage: http://www.iedb.org/assay/2019390
type:
Literature
publicationVenue:
Science
dates:
2013
study type: b cell assays
subject species: Hepatitis C virus (isolate H77)
fullName:
Leopold Kong
Erick Giang
Travis Nieusma
Rameshwar U Kadam
Kristin E Cogburn
Yuanzi Hua
Xiaoping Dai
Robyn L Stanfield
Dennis R Burton
Andrew B Ward
Ian A Wilson
Mansun Law
method:
ELISA
name:
Hepatitis C virus E2 envelope glycoprotein core structure.
description:
Binding of of epitope-specific AR3C Fab to the wild type E1E2 heterodimer was shown to be significantly reduced by substitutions 442FYQ444 to NYT or 428NCN430 to NCT. These substitutions also abrogated CD81 binding to E2, indicating the binding sites overlapped. Mutation L427Y reduced AR3C binding by 30% but abrogated CD81 binding. Epitope-specific AR3C Fab was also shown to bind the E2 construct by ELISA. The engineered E2c had truncations at the N and C termini, substitution of the potentially flexible variable region 2 (VR2, residues 400-485) with a Gly-Ser-Ser-Gly linker, and mutations N448D and N576D to remove glycosylation sites.