Related Experiment Video
Updated: Oct 2, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
An SR-protein induced by HSVI binding to cells functioning as a splicing inhibitor of viral pre-mRNA
Qihan Li1, Hongling Zhao, Li Jiang
1Institute of Medical Biology, Peking Union Medical College, Chinese Academy of Medical Sciences, 379# Jiaoling Road, Kunming, 650118, PRChina. qihanli@public.km.yn.cn
Abstract:
The interaction between a virus and its specific receptor on the membrane of the host cell mimics the physiological combination of signal ligand and its receptor, and initiates the specific signal transduction from this activated receptor to induce a relative gene response. During the investigation of the interaction between Herpes simplex virus I (HSVI) and human fibroblast via the virus binding to its receptor complex on the cellular membrane, a new gene of cellular response against the specific stimulation of HSVI binding to fibroblasts was cloned from a cDNA library established from mRNA of an early gene response. This gene encoded a protein of 14.9kDa with the structural characteristics of Arg-rich and RS repeats. The analysis of the role of this protein in the infection by HSVI indicated that this protein, expressed only in G(1)/S phase and phosphorylated, functioned as a splicing inhibitor of HSVI pre-mRNA. The details of the mechanism of this inhibition of HSVI pre-mRNA splicing is still unclear.
Related Concept Videos
siRNA - Small Interfering RNAs
In the cytoplasm, siRNA is processed from a double-stranded RNA, which comes from either endogenous DNA transcription or exogenous sources like a virus. This double-stranded RNA is then cleaved by the ATP-dependent...
Alternative RNA Splicing
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...
RNA Splicing
RNA Splicing
Herpes
Directing Proteins to the Rough Endoplasmic Reticulum

