Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1014884 |
| landingPage: |
http://www.iedb.org/assay/1658751 |
| type: |
Literature
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| publicationVenue: |
J Virol
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| dates: |
2009
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| study type: | b cell assays |
| subject species: | Hepatitis C virus |
| fullName: |
Zhen-yong Keck
Sophia H Li
Jinming Xia
Thomas von Hahn
Peter Balfe
Jane A McKeating
Jeroen Witteveldt
Arvind H Patel
Harvey Alter
Charles M Rice
Steven K H Foung
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| method: |
biological activity
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| name: |
Mutations in hepatitis C virus E2 located outside the CD81 binding sites lead to escape from broadly neutralizing antibodies but compromise virus infectivity.
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| description: |
The author provided accession AF009606 for the sequence source of the epitope.
Retrovirus particles pseudo-typed with HCV glycoproteins (HCVpp) isolated from sequential samples collected over a 26-year period from a chronically infected patient, H, were used to characterize the neutralization potential and binding affinity of a panel of anti-HCV E2 human mAbs. The binding affinities of the antibodies for the E2 conformational epitopes CBH-2, CBH-8C, CBH-5, HC-2, and HC-11 were improved 3-, 2.1-, 21.1-, 4.7-, and 4.8-fold, respectively, by N501S/A506V substitutions in the variant. As residues 501 and 506 are not known to be part of the epitopes identified by these antibodies, the findings are consistent with the view that residues 501 and 506 affect the E2 conformational structure required for these antibodies to bind to E2, as well as for E2 to bind to CD81.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
