ArticleNature communications2018
Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Preferential engagement of the anti-inflammatory ATP/adenosine axis by HIV vaccine candidate with V1-deleted envelope in male rhesus macaques.Cell reports. Medicine · 2026Article
- Explore antibody repertoire in the era of AI.Acta biochimica et biophysica Sinica · 2025Article
- A remarkable genetic shift in a transmitted/founder virus broadens antibody responses against HIV-1.eLife · 2024Article
- The V2 domain of HIV gp120 mimics an interaction between CD4 and integrin ⍺4β7.PLoS pathogens · 2023Article
- Broadly neutralizing antibody epitopes on HIV-1 particles are exposed after virus interaction with host cells.Journal of virology · 2023Article
- Article
- Cholera toxin B scaffolded, focused SIV V2 epitope elicits antibodies that influence the risk of SIVFrontiers in immunology · 2023Article
- An HIV-1 broadly neutralizing antibody overcomes structural and dynamic variation through highly focused epitope targeting.Npj viruses · 2023Article
- Differential V2-directed antibody responses in non-human primates infected with SHIVs or immunized with diverse HIV vaccines.Nature communications · 2022Article
- Structurally related but genetically unrelated antibody lineages converge on an immunodominant HIV-1 Env neutralizing determinant following trimer immunization.PLoS pathogens · 2021Article
- Anti-V2 antibodies virus vulnerability revealed by envelope V1 deletion in HIV vaccine candidates.iScience · 2021Article
- Mucosal integrin α4β7 blockade fails to reduce the seeding and size of viral reservoirs in SIV-infected rhesus macaques.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- To bnAb or Not to bnAb: Defining Broadly Neutralising Antibodies Against HIV-1.Frontiers in immunology · 2021Review
- HIV-1 Vaccine Sequences Impact V1V2 Antibody Responses: A Comparison of Two Poxvirus Prime gp120 Boost Vaccine Regimens.Scientific reports · 2020Article
- HIV vaccine delayed boosting increases Env variable region 2-specific antibody effector functions.JCI insight · 2020Article
- AAV-Mediated Expression of Broadly Neutralizing and Vaccine-like Antibodies Targeting the HIV-1 Envelope V2 Region.Molecular therapy. Methods & clinical development · 2019Article
- V2-Specific Antibodies in HIV-1 Vaccine Research and Natural Infection: Controllers or Surrogate Markers.Vaccines · 2019Review
- Multimeric Epitope-Scaffold HIV Vaccines Target V1V2 and Differentially Tune Polyfunctional Antibody Responses.Cell reports · 2019Article
- Vaccine-induced V1V2-specific antibodies control and or protect against infection with HIV, SIV and SHIV.Current opinion in HIV and AIDS · 2019Review
- Humoral Response to the HIV-1 Envelope V2 Region in a Thai Early Acute Infection Cohort.Cells · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The α4β7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated lymphoid tissues. Antibodies blocking this interaction early in infection can improve disease outcome, and V1V2-targeted antibodies were correlated with moderate efficacy reported from the RV144 HIV-1 vaccine trial. Monoclonal α4β7-blocking antibodies recognise two slightly different helical V2 conformations, and current structural data suggests their binding sites are occluded in prefusion envelope trimers. Here, we report cocrystal structures of two α4β7-blocking antibodies from an infected donor complexed with scaffolded V1V2 or V2 peptides. Both antibodies recognised the same helix-coil V2 conformation as RV144 antibody CH58, identifying a frequently sampled alternative conformation of full-length V1V2. In the context of Envelope, this α-helical form of V1V2 displays highly exposed α4β7-binding sites, potentially providing a functional role for non-native Envelope on virion or infected cell surfaces in HIV-1 dissemination, pathogenesis, and vaccine design.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.