The molecular basis of virus crossreactivity and neutralisation after immunisation with optimised chimeric peptides mimicking a putative helical epitope of the measles virus hemagglutinin protein.

Title:

The molecular basis of virus crossreactivity and neutralisation after immunisation with optimised chimeric peptides mimicking a putative helical epitope of the measles virus hemagglutinin protein.

Dataset

identifier:	1484075
description:	epitope description:KPNLSSKRSELSQLSMYRVF antigen name:Hemagglutinin glycoprotein host organism:Mus musculus BALB/c
aggregation:	instance of dataset
availability:	available
primaryPublications:	9881686

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1010186
landingPage:	http://www.iedb.org/assay/1484075

Publication

type:	Literature
publicationVenue:	Mol Immunol
dates:	1998

Dimension

study type:	b cell assays
subject species:	Measles virus strain Edmonston

Person

fullName:	K C El Kasmi D Theisen N H Brons C P Muller

Data Type

method:	antigen inhibition

Study

name:	The molecular basis of virus crossreactivity and neutralisation after immunisation with optimised chimeric peptides mimicking a putative helical epitope of the measles virus hemagglutinin protein.
description:	TB chimeras containing the MV F421-435 T helper epitope (TCE) linked to the B cell epitope (BCE) MV H236-255 generated anti-peptide antibodies, as well as anti-measles virus antibodies. Chimeras containing other TCEs (MV F256-270, F288-302, Pf CST3, TT830, LAC and Flu HA) were also examined, however the best results were achieved with MV F421-435. Sera which recognized specific residues on the peptides known to be surface exposed on MV (K242, E245, L246, Q248 and L249) also bound to the virus.

Data Repository

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

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