| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1001119 |
| landingPage: |
http://www.iedb.org/assay/1245746 |
| type: |
Literature
|
| publicationVenue: |
J Gen Virol
|
| dates: |
2005
|
| study type: | b cell assays |
| subject species: | Hendra henipavirus |
| fullName: |
John R White
Victoria Boyd
Gary S Crameri
Christine J Duch
Ryan K van Laar
Lin-Fa Wang
Bryan T Eaton
|
| method: |
biological activity
|
| name: |
Location of, immunogenicity of and relationships between neutralization epitopes on the attachment protein (G) of Hendra virus.
|
| description: |
Sites were identified on the globular head of the attachment glycoprotein (G) of Hendra virus (HeV) as contributing to a major epitope. Neutralizing mAbs were generated against HeV G and their biding sites were identified by sequencing the G gene of neutralization-escape variants selected by each mAb.
The ability of selected HeV G protein-specific mAbs to neutralize and bind virus was tested by standard serum neutralization assay and ELISA, respectively. MAb 3A5.D2 was capable of neutralizing and binding HeV virus. This mAb was not capable of neutralizing or binding to closely related Nipah virus (NiV). MAb 3A5.D2 was found to map to site V (aa385-386). Attempts (in a separate experiment) to use inhibition of mutual binding to define relationships between this and other mAbs were not strongly conclusive [Table 3].
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |