Effect of Mutations in the Human Immunodeficiency Virus Type 1 Protease on Cleavage of the gp41 Cytoplasmic Tail

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Published inJournal of Virology Vol. 84; no. 6; pp. 3121 - 3126
Main Authors WAHEED, Abdul A, ABLAN, Sherimay D, SOWDER, Raymond C, ROSER, James D, SCHAFFNER, Carl P, CHERTOVA, Elena, FREED, Eric O
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.03.2010
American Society for Microbiology (ASM)
Subjects
Amphotericin B - analogs & derivatives
Amphotericin B - pharmacology
Antifungal Agents - pharmacology
Biological and medical sciences
Drug Resistance, Viral - genetics
Fundamental and applied biological sciences. Psychology
HIV Envelope Protein gp41 - chemistry
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - metabolism
HIV Protease - genetics
HIV Protease - metabolism
HIV Protease Inhibitors - pharmacology
HIV-1 - drug effects
HIV-1 - enzymology
HIV-1 - genetics
Human immunodeficiency virus 1
Humans
Microbiology
Miscellaneous
Mutation
Virion - genetics
Virion - metabolism
Virology
Virus-Cell Interactions
Virus
Retroviridae
Human immunodeficiency virus
Mutation
HIV-1 virus
Lentivirus
Online AccessGet full text

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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList ABSTRACT We previously reported that human immunodeficiency virus type 1 (HIV-1) develops resistance to the cholesterol-binding compound amphotericin B methyl ester (AME) by acquiring mutations (P203L and S205L) in the cytoplasmic tail of the transmembrane envelope glycoprotein gp41 that create cleavage sites for the viral protease (PR). In the present study, we observed that a PR inhibitor-resistant (PIR) HIV-1 mutant is unable to efficiently cleave the gp41 cytoplasmic tail in P203L and S205L virions, resulting in loss of AME resistance. To define the pathway to AME resistance in the context of the PIR PR, we selected for resistance with an HIV-1 isolate expressing the mutant enzyme. We identified a new gp41 mutation, R236L, that results in cleavage of the gp41 tail by the PIR PR. These results highlight the central role of gp41 cleavage as the primary mechanism of AME resistance.
We previously reported that human immunodeficiency virus type 1 (HIV-1) develops resistance to the cholesterol-binding compound amphotericin B methyl ester (AME) by acquiring mutations (P203L and S205L) in the cytoplasmic tail of the transmembrane envelope glycoprotein gp41 that create cleavage sites for the viral protease (PR). In the present study, we observed that a PR inhibitor-resistant (PIR) HIV-1 mutant is unable to efficiently cleave the gp41 cytoplasmic tail in P203L and S205L virions, resulting in loss of AME resistance. To define the pathway to AME resistance in the context of the PIR PR, we selected for resistance with an HIV-1 isolate expressing the mutant enzyme. We identified a new gp41 mutation, R236L, that results in cleavage of the gp41 tail by the PIR PR. These results highlight the central role of gp41 cleavage as the primary mechanism of AME resistance.
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Author Carl P. Schaffner
Abdul A. Waheed
Eric O. Freed
James D. Roser
Sherimay D. Ablan
Raymond C. Sowder
Elena Chertova
AuthorAffiliation Virus-Cell Interaction Section, HIV Drug Resistance Program, NCI-Frederick, Frederick, Maryland 21702, 1 AIDS and Cancer Virus Program, SAIC/NCI-Frederick, Frederick, Maryland 21702, 2 Department of Microbiology and Biochemistry, The Waksman Institute, Rutgers—The State University of New Jersey, New Brunswick, New Jersey 08903 3
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
We previously reported that human immunodeficiency virus type 1 (HIV-1) develops resistance to the cholesterol-binding compound amphotericin B methyl ester...
ABSTRACT We previously reported that human immunodeficiency virus type 1 (HIV-1) develops resistance to the cholesterol-binding compound amphotericin B methyl...
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SubjectTerms Amphotericin B - analogs & derivatives
Amphotericin B - pharmacology
Antifungal Agents - pharmacology
Biological and medical sciences
Drug Resistance, Viral - genetics
Fundamental and applied biological sciences. Psychology
HIV Envelope Protein gp41 - chemistry
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - metabolism
HIV Protease - genetics
HIV Protease - metabolism
HIV Protease Inhibitors - pharmacology
HIV-1 - drug effects
HIV-1 - enzymology
HIV-1 - genetics
Human immunodeficiency virus 1
Humans
Microbiology
Miscellaneous
Mutation
Virion - genetics
Virion - metabolism
Virology
Virus-Cell Interactions
Title Effect of Mutations in the Human Immunodeficiency Virus Type 1 Protease on Cleavage of the gp41 Cytoplasmic Tail
URI http://jvi.asm.org/content/84/6/3121.abstract
https://www.ncbi.nlm.nih.gov/pubmed/20042499
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Volume 84
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