Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody.

Title:

Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody.

identifier:	1957691
description:	epitope description:QLINTNGSWHVN + PYRE(Q1) antigen name:Genome polyprotein host organism:Mus musculus BALB/c antibody name:AP33
aggregation:	instance of dataset
availability:	available
primaryPublications:	22993159

study type:	b cell assays
subject species:	Hepatitis C virus (isolate Glasgow)

fullName:	Jane A Potter Ania M Owsianka Nathan Jeffery David J Matthews Zhen-Yong Keck Patrick Lau Steven K H Foung Garry L Taylor Arvind H Patel

method:	ELISA

name:	Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody.
description:	The N-terminal Gln residue is a pyroglutamic acid residue. The epitope-specific mAb AP33 bound to HCV E2 by ELISA. Single alanine substitution of 15 antibody residues in close proximity to the epitope in the crystal structure showed that mutations Y(H)33A, Y(H)50A, Y(H)58A, I(H)95A, Y(H)100A, F(L)32A, N(L)91A and W(L)96A resulted in a greater than 90% reduction of E2 binding relative to WT. Mutant N(L)92A showed 40% reduced binding. Alanine-scanning mutagenesis of E2 residues confirmed that L413, N415, G418 and W420 in the epitope sequence were important for AP33 binding. Mutation of residues outside the epitope appear to disrupt E2 conformation, but L654 was identified as a possible additional contact residue.

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

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