Novel Ring Structure in the gp41 Trimer of Human Immunodeficiency Virus Type 1 That Modulates Sensitivity and Resistance to Broadly Neutralizing Antibodies

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Published inJournal of Virology Vol. 83; no. 15; pp. 7728 - 7738
Main Authors O'ROURKE, Sara M, SCHWEIGHARDT, Becky, SCOTT, William G, WRIN, Terri, FONSECA, Dora P. A. J, SINANGIL, Faruk, BERMAN, Phillip W
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.08.2009
American Society for Microbiology (ASM)
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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 The identification of the determinants of sensitivity and resistance to broadly neutralizing antibodies is a high priority for human immunodeficiency virus (HIV) research. An analysis of the swarm of closely related envelope protein variants in an HIV-infected individual revealed a mutation that markedly affected sensitivity to neutralization by antibodies and antiviral entry inhibitors targeting both gp41 and gp120. This mutation mapped to the C34 helix of gp41 and disrupted an unexplored structural feature consisting of a ring of hydrogen bonds in the gp41 trimer. This mutation appeared to affect the assembly of the six-helix bundle required for virus fusion and to alter the conformational equilibria so as to favor the prehairpin intermediate conformation required for the binding of the membrane proximal external region-specific neutralizing antibodies 2F5 and 4E10 and the antiviral drug enfuvirtide (Fuzeon). The QUOTATION_MARKswarm analysisQUOTATION_MARK method we describe furthers our understanding of the relationships among the structure, function, and antigenicity of the HIV envelope protein and represents a new approach to the identification of vaccine antigens.
The identification of the determinants of sensitivity and resistance to broadly neutralizing antibodies is a high priority for human immunodeficiency virus (HIV) research. An analysis of the swarm of closely related envelope protein variants in an HIV-infected individual revealed a mutation that markedly affected sensitivity to neutralization by antibodies and antiviral entry inhibitors targeting both gp41 and gp120. This mutation mapped to the C34 helix of gp41 and disrupted an unexplored structural feature consisting of a ring of hydrogen bonds in the gp41 trimer. This mutation appeared to affect the assembly of the six-helix bundle required for virus fusion and to alter the conformational equilibria so as to favor the prehairpin intermediate conformation required for the binding of the membrane proximal external region-specific neutralizing antibodies 2F5 and 4E10 and the antiviral drug enfuvirtide (Fuzeon). The "swarm analysis" method we describe furthers our understanding of the relationships among the structure, function, and antigenicity of the HIV envelope protein and represents a new approach to the identification of vaccine antigens.
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Author Faruk Sinangil
Becky Schweighardt
Phillip W. Berman
Terri Wrin
William G. Scott
Sara M. O'Rourke
Dora P. A. J. Fonseca
AuthorAffiliation Department of Biomolecular Engineering, University of California, Santa Cruz, California 95064, 1 Monogram Biosciences, South San Francisco, California 94080, 2 Department of Chemistry and Biochemistry, University of California Santa Cruz, Santa Cruz, California 95064, 3 Global Solutions for Infectious Diseases, South San Francisco, California 94080 4
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Issue 15
Keywords Immunopathology
HIV-1 virus
Retroviridae
AIDS
Immune deficiency
Lentivirus
Neutralizing antibody
Virology
Infection
Virus
Sensitivity resistance
Viral disease
Human immunodeficiency virus
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Corresponding author. Mailing address: Department of Biomolecular Engineering, Baskin School of Engineering, University of California, Santa Cruz, 1156 High Street, MS-SOE2, Santa Cruz, CA 95064. Phone: (831) 459-3529. Fax: (831) 459-1970. E-mail: pwb@soe.ucsc.edu
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  doi: 10.1128/AAC.00853-06
– ident: e_1_3_2_44_2
  doi: 10.1097/QAI.0b013e318074eb5a
– ident: e_1_3_2_7_2
  doi: 10.1371/journal.pmed.0050009
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The identification of the determinants of sensitivity and resistance to broadly neutralizing antibodies is a high priority for human immunodeficiency virus...
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StartPage 7728
SubjectTerms Amino Acid Sequence
Antibodies, Viral - immunology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
HIV Envelope Protein gp41 - chemistry
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - immunology
HIV Infections - immunology
HIV Infections - virology
HIV-1 - chemistry
HIV-1 - genetics
HIV-1 - immunology
Human immunodeficiency virus 1
Humans
Microbiology
Miscellaneous
Molecular Conformation
Molecular Sequence Data
Mutation
Neutralization Tests
Pathogenesis and Immunity
Protein Conformation
Virology
Title Novel Ring Structure in the gp41 Trimer of Human Immunodeficiency Virus Type 1 That Modulates Sensitivity and Resistance to Broadly Neutralizing Antibodies
URI http://jvi.asm.org/content/83/15/7728.abstract
https://www.ncbi.nlm.nih.gov/pubmed/19474108
https://search.proquest.com/docview/21325118
https://search.proquest.com/docview/67466321
https://pubmed.ncbi.nlm.nih.gov/PMC2708639
Volume 83
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