Mutation at a Single Position in the V2 Domain of the HIV-1 Envelope Protein Confers Neutralization Sensitivity to a Highly Neutralization-Resistant Virus

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Published inJournal of Virology Vol. 84; no. 21; pp. 11200 - 11209
Main Authors O'ROURKE, Sara M, SCHWEIGHARDT, Becky, PHUNG, Pham, FONSECA, Dora P. A. J, TERRY, Karianne, WRIN, Terri, SINANGIL, Faruk, BERMAN, Phillip W
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.11.2010
American Society for Microbiology (ASM)
Subjects
Antibodies, Viral - pharmacology
Antigen-Antibody Reactions
Biological and medical sciences
Epitopes
Fundamental and applied biological sciences. Psychology
HIV Envelope Protein gp120 - genetics
HIV Envelope Protein gp120 - immunology
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - immunology
Human immunodeficiency virus 1
Humans
Integrins - metabolism
Microbiology
Miscellaneous
Mutation, Missense
Neutralization Tests
Pathogenesis and Immunity
Protein Conformation - drug effects
Simian immunodeficiency virus
Virology
Virus
Resistance
Sensitivity
HIV-1 virus
Retroviridae
Human immunodeficiency virus
Mutation
Lentivirus
Protein
Neutralization
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Understanding the determinants of neutralization sensitivity and resistance is important for the development of an effective human immunodeficiency virus type 1 (HIV-1) vaccine. In these studies, we have made use of the swarm of closely related envelope protein variants (quasispecies) from an extremely neutralization-resistant clinical isolate in order to identify mutations that conferred neutralization sensitivity to antibodies in sera from HIV-1-infected individuals. Here, we describe a virus with a rare mutation at position 179 in the V2 domain of gp120, where replacement of aspartic acid (D) by asparagine (N) converts a virus that is highly resistant to neutralization by multiple polyclonal and monoclonal antibodies, as well as antiviral entry inhibitors, to one that is sensitive to neutralization. Although the V2 domain sequence is highly variable, D at position 179 is highly conserved in HIV-1 and simian immunodeficiency virus (SIV) and is located within the LDI/V recognition motif of the recently described α4β7 receptor binding site. Our results suggest that the D179N mutation induces a conformational change that exposes epitopes in both the gp120 and the gp41 portions of the envelope protein, such as the CD4 binding site and the MPER, that are normally concealed by conformational masking. Our results suggest that D179 plays a central role in maintaining the conformation and infectivity of HIV-1 as well as mediating binding to α4β7.
Understanding the determinants of neutralization sensitivity and resistance is important for the development of an effective human immunodeficiency virus type 1 (HIV-1) vaccine. In these studies, we have made use of the swarm of closely related envelope protein variants (quasispecies) from an extremely neutralization-resistant clinical isolate in order to identify mutations that conferred neutralization sensitivity to antibodies in sera from HIV-1-infected individuals. Here, we describe a virus with a rare mutation at position 179 in the V2 domain of gp120, where replacement of aspartic acid (D) by asparagine (N) converts a virus that is highly resistant to neutralization by multiple polyclonal and monoclonal antibodies, as well as antiviral entry inhibitors, to one that is sensitive to neutralization. Although the V2 domain sequence is highly variable, D at position 179 is highly conserved in HIV-1 and simian immunodeficiency virus (SIV) and is located within the LDI/V recognition motif of the recently described 4?7 receptor binding site. Our results suggest that the D179N mutation induces a conformational change that exposes epitopes in both the gp120 and the gp41 portions of the envelope protein, such as the CD4 binding site and the MPER, that are normally concealed by conformational masking. Our results suggest that D179 plays a central role in maintaining the conformation and infectivity of HIV-1 as well as mediating binding to 4?7.
Author Faruk Sinangil
Becky Schweighardt
Phillip W. Berman
Terri Wrin
Pham Phung
Karianne Terry
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 Global Solutions for Infectious Diseases, South San Francisco, California 94080 3
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Issue 21
Keywords Virus
Resistance
Sensitivity
HIV-1 virus
Retroviridae
Human immunodeficiency virus
Mutation
Lentivirus
Protein
Neutralization
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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...
Understanding the determinants of neutralization sensitivity and resistance is important for the development of an effective human immunodeficiency virus type...
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SubjectTerms Antibodies, Viral - pharmacology
Antigen-Antibody Reactions
Biological and medical sciences
Epitopes
Fundamental and applied biological sciences. Psychology
HIV Envelope Protein gp120 - genetics
HIV Envelope Protein gp120 - immunology
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - immunology
Human immunodeficiency virus 1
Humans
Integrins - metabolism
Microbiology
Miscellaneous
Mutation, Missense
Neutralization Tests
Pathogenesis and Immunity
Protein Conformation - drug effects
Simian immunodeficiency virus
Virology
Title Mutation at a Single Position in the V2 Domain of the HIV-1 Envelope Protein Confers Neutralization Sensitivity to a Highly Neutralization-Resistant Virus
URI http://jvi.asm.org/content/84/21/11200.abstract
https://www.ncbi.nlm.nih.gov/pubmed/20702624
https://search.proquest.com/docview/757177946
https://search.proquest.com/docview/762272487
https://pubmed.ncbi.nlm.nih.gov/PMC2953176
Volume 84
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