Immunological Data Discovery Index
Advanced Search
identifier: 14923
description:
epitope description:L271
antigen name:Genome polyprotein
host organism:Mus musculus BALB/c
antibody name:P1D8
aggregation:
instance of dataset
availability:
available
primaryPublications: 11900844
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/872
landingPage: http://www.iedb.org/assay/14923
type:
Literature
publicationVenue:
Virus Res
dates:
2002
study type: b cell assays
subject species: Bovine viral diarrhea virus strain Trangie Y546
fullName:
L M Brown
R A Papa
M J Frost
S G Mackintosh
X Gu
R J Dixon
A D Shannon
method:
ELISA
name:
A single amino acid is critical for the expression of B-cell epitopes on the helicase domain of the pestivirus NS3 protein.
description:
As the title of this article states, this Leucine1858 residue is critical for recognition of BVDV-1 isolates by mAb P1D8. Position is relative to SD-1 polyprotein. Genbank accesion is for virus polyprotien.
Binding by monoclonal antibodies P1D8, P1H11 and P4A11 to recombinant source protein is abolished if aa 1858 is a Valine or a Serine (Hay and NZ 97-360 strains) and when that residue is mutated to Leucine, as in the Trangie strain, reactivity is recovered. mAb P1D8 is specific for all BVDV-1 isolates where aa1858 is a Leucine (i.e. except for Hay and NZ 97-360 strains). The reactivity of P1H11 and P4A11, pestivirus specific antibodies, is also dependent on this aa in BVDV-1 isolates, but not in BVDV-2, BDV or CSFV isolates. That aa lateral chain is shown in protein modeling analysis to protrude on the surface of the protein.

Feedback?

If you are having problems using our tools, or if you would just like to send us some feedback, please post your questions on Feedback.