ArticleThe Journal of biological chemistry2008
The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 90 citations in OpenAlex.
- Heparan sulfate as an attachment factor for ASFV is restricted by host HB-EGF.Cellular and molecular life sciences : CMLS · 2026Article
- Probing Glycosaminoglycan-Protein Interactions: Applications of Surface Plasmon Resonance.Biosensors · 2026Review
- Phospho-Chitooligosaccharides below 1 kDa Inhibit HIV-1 Entry In Vitro.Current issues in molecular biology · 2024Article
- Article
- In Vitro Anti-HIV-1 Activity of Chitosan OligomersBiotech (Basel (Switzerland)) · 2023Article
- Red Algal Sulfated Galactan Binds and Protects Neural Cells from HIV-1 gp120 and Tat.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Sulfated Non-Saccharide Glycosaminoglycan Mimetics as Novel Drug Discovery Platform for Various Pathologies.Current medicinal chemistry · 2020Review
- Angiogenesis, Lymphangiogenesis, and the Immune Response in South African Preeclamptic Women Receiving HAART.International journal of molecular sciences · 2019Review
- Determinants of Tenascin-C and HIV-1 envelope binding and neutralization.Mucosal immunology · 2019Article
- Conformational changes in Chikungunya virus E2 protein upon heparan sulfate receptor binding explain mechanism of E2-E1 dissociation during viral entry.Bioscience reports · 2019Article
- Sulfotransferase and Heparanase: Remodeling Engines in Promoting Virus Infection and Disease Development.Frontiers in pharmacology · 2018Review
- Sulfated Glycans and Related Digestive Enzymes in the Zika Virus Infectivity: Potential Mechanisms of Virus-Host Interaction and Perspectives in Drug Discovery.Interdisciplinary perspectives on infectious diseases · 2017Review
- Inhibition of Human Metapneumovirus Binding to Heparan Sulfate Blocks Infection in Human Lung Cells and Airway Tissues.Journal of virology · 2016Article
- CD4-mimetic sulfopeptide conjugates display sub-nanomolar anti-HIV-1 activity and protect macaques against a SHIV162P3 vaginal challenge.Scientific reports · 2016Article
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- Article
- HIV-1 entry in SupT1-R5, CEM-ss, and primary CD4+ T cells occurs at the plasma membrane and does not require endocytosis.Journal of virology · 2014Article
- Human immunodeficiency virus and heparan sulfate: from attachment to entry inhibition.Frontiers in immunology · 2013Review
- Tenascin-C is an innate broad-spectrum, HIV-1-neutralizing protein in breast milk.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Genetic diversity of the highly variable V1 region interferes with Human Immunodeficiency Virus type 1 envelope functionality.Retrovirology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is well established that the human immunodeficiency virus-1 envelope glycoprotein surface unit, gp120, binds to cell-associated heparan sulfate (HS). Virus infectivity is increased by such interaction, and a variety of soluble polyanions efficiently neutralize immunodeficiency virus-1 in vitro. This interaction has been mainly attributed to the gp120 V3 loop. However, although evidence suggested that this particular domain does not fully recapitulate the binding activity of the protein, the ability of HS to bind to other regions of gp120 has not been completely addressed, and the exact localizations of the polysaccharide binding sites are not known. To investigate in more detail the structural basis of the HS-gp120 interaction, we used a mapping strategy and compared the heparin binding activity of wild type and mutant gp120 using surface plasmon resonance-based binding assays. Four heparin binding domains (1-4) were identified in the V2 and V3 loops, in the C-terminal domain, and within the CD4-induced bridging sheet. Interestingly, three of them were found in domains of the protein that undergo structural changes upon binding to CD4 and are involved in co-receptor recognition. In particular, Arg(419), Lys(421), and Lys(432), which directly interact with the co-receptor, are targeted by heparin. This study provides a complete account of the gp120 residues involved in heparin binding and identified several binding surfaces that constitute potential target for viral entry inhibition.
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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.