|
Basic Characteristics of Mutations
|
|
Mutation Site
|
K303N |
|
Mutation Site Sentence
|
Reconstruction of a plaque-purified revertant which contained Gly360 and additional substitutions (Asn for Lys303 and Val for Ala261) yielded a virus whose infectious center size, growth efficiency, and cell penetration rate similar to the parental YF5.2iv virus, whereas viruses with Asn303 or Val261 alone with Gly360 yielded either a small-plaque virus or a parental revertant. |
|
Mutation Level
|
Amino acid level |
|
Mutation Type
|
Nonsynonymous substitution |
|
Gene/Protein/Region
|
E |
|
Standardized Encoding Gene
|
envelope
|
|
Genotype/Subtype
|
- |
|
Viral Reference
|
-
|
|
Functional Impact and Mechanisms
|
|
Disease
|
Cell line
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
- |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
15327896
|
|
Title
|
Yellow fever 17D virus: pseudo-revertant suppression of defective virus penetration and spread by mutations in domains II and III of the E protein
|
|
Author
|
Vlaycheva L,Nickells M,Droll DA,Chambers TJ
|
|
Journal
|
Virology
|
|
Journal Info
|
2004 Sep 15;327(1):41-9
|
|
Abstract
|
A yellow fever (YFV) 17D virus variant, which causes persistent infection of mouse neuroblastoma cells associated with defective cell penetration and small plaque size, yielded plaque-revertant viruses from cells transfected with viral transcripts encoding the adaptive mutation (Gly360 in the E protein). Reconstruction of a plaque-purified revertant which contained Gly360 and additional substitutions (Asn for Lys303 and Val for Ala261) yielded a virus whose infectious center size, growth efficiency, and cell penetration rate similar to the parental YF5.2iv virus, whereas viruses with Asn303 or Val261 alone with Gly360 yielded either a small-plaque virus or a parental revertant. These data indicate that the YFV E protein is subject to suppression of mutations in domain III that are deleterious for viral entry and spread by a second-site mutation in domain II. Position 261 lies within the hydrophobic ligand-binding pocket at the domain I-II interface, a site believed to be involved in the hinge-like conformational change of domain II during activation of membrane fusion-activity. Results of this study provide genetic data consistent with findings on flavivirus structure and implicate domain III in functions beyond simply cell surface attachment.
|
|
Sequence Data
|
-
|