Document Detail

Functional integrity of naturally occurring mutants of HIV-1 subtype C Vpr.
MedLine Citation:
PMID:  20801175     Owner:  NLM     Status:  MEDLINE    
HIV-1 Vpr, an accessory protein with multiple functions, is involved in the induction of apoptosis, cell cycle G2 arrest, and modulation of gene expression. Many functions of this protein have been documented for the wild-type subtype B Vpr, however the functionality of other subtypes has not sufficiently been addressed. In this study, the functionality of Subtype B Vpr, 6 subtype C mutant Vpr proteins and the consensus sequence of subtype C Vpr were compared with each other. All the subtype B and C Vpr proteins localized to the nucleus of human 293T cells. Subtype C Vpr proteins induced cell cycle G2 arrest in a lower proportion of human 293T cells compared to subtype B Vpr. Subtype B and the naturally mutant Vpr proteins induced apoptosis in a similar manner, ranging from 95.33% to 98.64%. However, an artificially designed Vpr protein containing the consensus sequences of subtype C Vpr indicated a reduced ability in induction of apoptosis. The study of mRNA profile of the transfected cells indicated that all Vpr proteins modulated the apoptotic genes triggering the intrinsic pathway of apoptosis. Our results indicate that subtype C Vpr is able to exert the same functions previously reported for subtype B Vpr. Most natural mutations in Vpr not only do not disturb the functions of the protein but also potentiate the protein for an increased functionality. The natural mutations of Vpr may thus not always be regarded as defective mutations. The study suggests the adaptive role of the natural mutations commonly found in subtype C Vpr.
Bizhan Romani; Richard H Glashoff; Susan Engelbrecht
Related Documents :
21137065 - Differential regulation of redox proteins and chaperones in hbeβ-thalassemia erythrocy...
18603135 - Dissection of the bcl-2 family signaling network with stabilized alpha-helices of bcl-2...
25053255 - Ram seminal plasma proteome and its impact on liquid preservation of spermatozoa.
10428475 - 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves.
16361095 - Molecular mechanisms of dendritic spine morphogenesis.
17020825 - Heterogeneity of protein conformation in solution from the lifetime of tryptophan phosp...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-08-27
Journal Detail:
Title:  Virus research     Volume:  153     ISSN:  1872-7492     ISO Abbreviation:  Virus Res.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-10-04     Completed Date:  2011-01-13     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8410979     Medline TA:  Virus Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  288-98     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier B.V. All rights reserved.
Division of Medical Virology, Department of Pathology, University of Stellenbosch, Tygerberg 7505, South Africa.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Cell Line
Cell Nucleus / chemistry
Gene Expression Profiling
HIV-1 / genetics,  pathogenicity*
Mutant Proteins / genetics*,  metabolism*
vpr Gene Products, Human Immunodeficiency Virus / genetics*,  metabolism*
Reg. No./Substance:
0/Mutant Proteins; 0/vpr Gene Products, Human Immunodeficiency Virus; 0/vpr protein, Human immunodeficiency virus 1

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Enhanced transduction efficiency of fiber-substituted adenovirus vectors by the incorporation of RGD...
Next Document:  The infection of mammalian and insect cells with SFV bearing nsP1 palmitoylation mutations.