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