ArticleVirology2017
Glycosylation and oligomeric state of envelope protein might influence HIV-1 virion capture by α4β7 integrin.
Article in Virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Targeted bacteriophage T4 nanoparticles reverse HIV-1 latency in human T cell line models.iScience · 2025Article
- HIV broadly neutralizing antibody precursors to the Apex epitope induced in nonhuman primates.Science immunology · 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
- Article
- Abiological catalysis by myoglobin mutant with a genetically incorporated unnatural amino acid.The Biochemical journal · 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
- Primary HIV-1 and Infectious Molecular Clones Are Differentially Susceptible to Broadly Neutralizing Antibodies.Vaccines · 2020Article
- 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
- A sequestered fusion peptide in the structure of an HIV-1 transmitted founder envelope trimer.Nature communications · 2019Article
- Common helical V1V2 conformations of HIV-1 Envelope expose the α4β7 binding site on intact virions.Nature communications · 2018Article
- Select gp120 V2 domain specific antibodies derived from HIV and SIV infection and vaccination inhibit gp120 binding to α4β7.PLoS pathogens · 2018Article
- The Role of Integrin αCurrent HIV/AIDS reports · 2018Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
The α4ß7 integrin present on host cells recognizes the V1V2 domain of the HIV-1 envelope protein. This interaction might be involved in virus transmission. Administration of α4ß7-specific antibodies inhibit acquisition of SIV in a macaque challenge model. But the molecular details of V1V2: α4ß7 interaction are unknown and its importance in HIV-1 infection remains controversial. Our biochemical and mutational analyses show that glycosylation is a key modulator of V1V2 conformation and binding to α4ß7. Partially glycosylated, but not fully glycosylated, envelope proteins are preferred substrates for α4ß7 binding. Surprisingly, monomers of the envelope protein bound strongly to α4ß7 whereas trimers bound poorly. Our results suggest that a conformationally flexible V1V2 domain allows binding of the HIV-1 virion to the α4ß7 integrin, which might impart selectivity for the poorly glycosylated HIV-1 envelope containing monomers to be more efficiently captured by α4ß7 integrin present on mucosal cells at the time of HIV-1 transmission.
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Registered trials
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