JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Piller, S. C.
Right arrow Articles by Hunter, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Piller, S. C.
Right arrow Articles by Hunter, E.

 Previous Article  |  Next Article 

Journal of Virology, December 2000, p. 11717-11723, Vol. 74, No. 24
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Mutational Analysis of Conserved Domains within the Cytoplasmic Tail of gp41 from Human Immunodeficiency Virus Type 1: Effects on Glycoprotein Incorporation and Infectivity

Sabine C. Piller, John W. Dubay, Cynthia A. Derdeyn, and Eric Hunter*

Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294

Received 25 February 2000/Accepted 25 September 2000

The transmembrane (TM) glycoprotein gp41 of human immunodeficiency virus type 1 possesses an unusually long (~150 amino acids) and highly conserved cytoplasmic region. Previous studies in which this cytoplasmic tail had been deleted partially or entirely have suggested that it is important for virus infectivity and incorporation of the gp120-gp41 glycoprotein complex into virions. To determine which regions of the conserved C-terminal domains are important for glycoprotein incorporation and infectivity, several small deletions and amino acid substitutions which modify highly conserved motifs were constructed in the infectious proviral background of NL4.3. The effects of these mutations on infectivity and glycoprotein incorporation into virions produced from transfected 293-T cells and infected H9 and CEM×174 cells were determined. With the exception of a mutation deleting amino acids QGL, all of the constructs resulted in decreased infectivity of the progeny virus both in a single-round infectivity assay and in a multiple-infection assay in H9 and CEM×174 cells. For most mutations, the decreased infectivity was correlated with a decreased incorporation of glycoprotein into virions. Substitution of the arginines (residues 839 and 846) with glutamates also reduced infectivity, but without a noticeable decrease in the amount of glycoprotein incorporated into virus produced from infected T cells. These results demonstrate that minor alterations in the conserved C-terminal region of the gp41 cytoplasmic tail can result in reductions in infectivity that correlate for most but not all constructs with a decrease in glycoprotein incorporation. Observed cell-dependent differences suggest the involvement of cellular factors in regulating glycoprotein incorporation and infectivity.

* Corresponding author. Mailing address: Center for AIDS Research, University of Alabama at Birmingham, Bevill Biomedical Research Building, Rm. 256D, 845 19th St. South, Birmingham, AL 35294-2170. Phone: (205) 934-4321. Fax: (205) 934-1640. E-mail: ehunter{at}uab.edu.

Journal of Virology, December 2000, p. 11717-11723, Vol. 74, No. 24
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2000 by the American Society for Microbiology. All rights reserved.