|
Basic Characteristics of Mutations
|
|
Mutation Site
|
R158A |
|
Mutation Site Sentence
|
A R158A/R161A double substitution in pUL34 has been shown to strongly inhibit both nuclear egress and spread. |
|
Mutation Level
|
Amino acid level |
|
Mutation Type
|
Nonsynonymous substitution |
|
Gene/Protein/Region
|
UL34 |
|
Standardized Encoding Gene
|
UL34
|
|
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
|
37787529
|
|
Title
|
Extragenic suppression of an HSV-1 UL34 nuclear egress mutant reveals role for pUS9 as an inhibitor of epithelial cell-to-cell spread
|
|
Author
|
Twigg CAI,Haugo-Crooks A,Roller RJ
|
|
Journal
|
Journal of virology
|
|
Journal Info
|
2023 Oct 31;97(10):e0083623
|
|
Abstract
|
Herpesviruses are able to disseminate in infected hosts despite development of a strong immune response. Their ability to do this relies on a specialized process called cell-to-cell spread in which newly assembled virus particles are trafficked to plasma membrane surfaces that abut adjacent uninfected cells. The mechanism of cell-to-cell spread is obscure, and little is known about whether or how it is regulated in different cells. We show here that a viral protein with a well-characterized role in promoting spread from neurons has an opposite, inhibitory role in other cells.
|
|
Sequence Data
|
-
|