ArticleProceedings of the National Academy of Sciences of the United States of America2001
The role of the third beta strand in gp120 conformation and neutralization sensitivity of the HIV-1 primary isolate DH012.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Regulation of epitope exposure in the gp41 membrane-proximal external region through interactions at the apex of HIV-1 Env.PLoS pathogens · 2022Article
- Structural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting.Biochemistry · 2017Article
- Article
- Anti-AIDS agents 90. novel C-28 modified bevirimat analogues as potent HIV maturation inhibitors.Journal of medicinal chemistry · 2012Article
- Design and characterization of a peptide mimotope of the HIV-1 gp120 bridging sheet.International journal of molecular sciences · 2012Article
- The role of dynamin in HIV type 1 Env-mediated cell-cell fusion.AIDS research and human retroviruses · 2011Article
- A conserved determinant in the V1 loop of HIV-1 modulates the V3 loop to prime low CD4 use and macrophage infection.Journal of virology · 2011Article
- Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization.Journal of virology · 2010Article
- Neutralization patterns and evolution of sequential HIV type 1 envelope sequences in HIV type 1 subtype B-infected drug-naive individuals.AIDS research and human retroviruses · 2008Article
- Betulinic acid derivatives that target gp120 and inhibit multiple genetic subtypes of human immunodeficiency virus type 1.Antimicrobial agents and chemotherapy · 2008Article
- Article
- NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.The Biochemical journal · 2005Article
- The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection.Journal of virology · 2004Article
- Bifunctional anti-human immunodeficiency virus type 1 small molecules with two novel mechanisms of action.Antimicrobial agents and chemotherapy · 2004Article
- A novel human antibody against human immunodeficiency virus type 1 gp120 is V1, V2, and V3 loop dependent and helps delimit the epitope of the broadly neutralizing antibody immunoglobulin G1 b12.Journal of virology · 2003Article
- Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120.Journal of virology · 2003Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Neutralization of HIV-1 primary isolates has been a tremendous challenge for AIDS vaccine development. Here, we identify a single amino acid change (T198P) in gp120 that alters the neutralization sensitivity of the primary isolate DH012 to antibodies against multiple neutralization epitopes that include the V3, CD4-induced, and CD4 binding sites in gp120. This mutation is located in the V1/V2 stem region that forms the third beta strand (beta3) of the bridging sheet of gp120. The conformation of variable loops, especially V1/V2 and V3, was proposed to regulate the accessibility of these neutralization epitopes. The results of this study indicate a direct association between the V1/V2 and V3 loops of DH012 gp120. The single amino acid mutation T198P in the beta3 severely compromises the interaction between the V1/V2 and V3 loops. These results suggest that interaction of V1/V2 and V3 can mask the neutralization epitopes and that the beta3 plays a critical role in determining the neutralization sensitivity by modulating the interaction. This study provides an insight into why primary isolates are relatively resistant to antibody neutralization and might facilitate the development of anti-HIV strategies against HIV-1 infection.
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