J Gen Virol Try IJSEM Online
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
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 Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pelemans, H.
Right arrow Articles by Balzarini, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pelemans, H.
Right arrow Articles by Balzarini, J.
Agricola
Right arrow Articles by Pelemans, H.
Right arrow Articles by Balzarini, J.

Journal of General Virology, Vol 79, 1347-1352, Copyright © 1998 by Society for General Microbiology

ARTICLES

A proline-to-histidine substitution at position 225 of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) sensitizes HIV-1 RT to BHAP U-90152

H Pelemans, RM Esnouf, MA Parniak, AM Vandamme, E De Clercq and J Balzarini
Rega Institute for Medical Research, Katholieke Universiteit Leuven, Belgium.

Two mutant virus strains in which the novel P225H mutation appeared in a V106A reverse transcriptase (RT)-mutated genetic background upon treatment of human immunodeficiency virus type 1 (HIV-1) with quinoxaline S-2720 were isolated. Surprisingly, the addition of the P225H mutation to the V106A RT mutant genetic background resensitized the V106A RT mutant virus to the non-nucleoside RT inhibitor (NNRTI) BHAP U-90152, but not to other NNRTIs. Construction of both recombinant viruses and recombinant RTs containing the V106A, P225H and V106A+P225H mutations revealed that P225H was indeed responsible for the marked potentiation of the antiviral activity of BHAP against the P225H single- mutant virus and the V106A+P225H double-mutant virus when compared to wild-type and V106A single-mutant viruses, respectively. An explanation for the markedly increased sensitivity of the P225H mutant HIV-1 RT to BHAP and not to the other NNRTIs was provided by the unique features of the X-ray structure of the RT-BHAP complex.


This article has been cited by other articles:


Home page
 Clin. Microbiol. Rev.Home page
R. W. Shafer
Genotypic Testing for Human Immunodeficiency Virus Type 1 Drug Resistance
Clin. Microbiol. Rev., April 1, 2002; 15(2): 247 - 277.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Pelemans, R. M. Esnouf, H. Jonckheere, E. De Clercq, and J. Balzarini
Mutational Analysis of Tyr-318 within the Non-nucleoside Reverse Transcriptase Inhibitor Binding Pocket of Human Immunodeficiency Virus Type I Reverse Transcriptase
J. Biol. Chem., December 18, 1998; 273(51): 34234 - 34239.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1998 by the Society for General Microbiology.