Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III.

Abstract:

:West Nile virus (WNV) is a mosquito-borne flavivirus that causes febrile illness, encephalitis, and occasionally death in humans. The envelope protein is the main component of the WNV virion surface, and domain III of the envelope protein (EIII) is both a putative receptor binding domain and a target of highly specific, potently neutralizing antibodies. Envelope E-332 (E-332) is known to have naturally occurring variation and to be a key determinant of neutralization for anti-EIII antibodies. A panel of viruses containing all possible amino acid substitutions at E-332 was constructed. E-332 was found to be highly tolerant of mutation, and almost all of these changes had large impacts on antigenicity of EIII but only limited effects on growth or virulence phenotypes.

journal_name

Virology

journal_title

Virology

authors

Plante JA,Torres M,Huang CY,Beasley DWC

doi

10.1016/j.virol.2016.05.024

subject

Has Abstract

pub_date

2016-09-01 00:00:00

pages

97-105

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(16)30133-7

journal_volume

496

pub_type

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