ArticleJournal of virology2012
Structural basis of ligand interactions of the large extracellular domain of tetraspanin CD81.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
The trial behind it
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
29 citing papers in PubMed, 49 citations in OpenAlex.
- Conserved use of tetraspanin CD9 as an entry receptor by rhabdoviruses spanning multiple genera.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Tetraspanin SfCD9 as a Key Membrane Binding Factor of SRBSDV P10 Facilitates Viral Entry Into Sogatella furcifera Midgut Epithelial Cells via Clathrin-Mediated Endocytosis.Molecular plant pathology · 2025Article
- Tetraspanins: structure, dynamics, and principles of partner-protein recognition.Trends in cell biology · 2024Review
- Review
- A molecular docking exploration of the large extracellular loop of tetraspanin CD81 with small molecules.In silico pharmacology · 2024Article
- Targeting of Tetraspanin CD81 with Monoclonal Antibodies and Small Molecules to Combat Cancers and Viral Diseases.Cancers · 2023Review
- The large extracellular loop is important for recruiting CD63 to exosomes.microPublication biology · 2023Article
- Construction of Yeast Display Libraries for Selection of Antigen-Binding Variants of Large Extracellular Loop of CD81, a Major Surface Marker Protein of Extracellular Vesicles.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Open conformation of tetraspanins shapes interaction partner networks on cell membranes.The EMBO journal · 2020Article
- A dynamic interaction between CD19 and the tetraspanin CD81 controls B cell co-receptor trafficking.eLife · 2020Article
- Hepatitis C Virus Structure: Defined by What It Is Not.Cold Spring Harbor perspectives in medicine · 2020Review
- High Yield Expression of Recombinant CD151 in E. coli and a Structural Insight into Cholesterol Binding Domain.Molecular biotechnology · 2019Article
- The Septate Junction Protein Tsp2A Restricts Intestinal Stem Cell Activity via Endocytic Regulation of aPKC and Hippo Signaling.Cell reports · 2019Article
- Inhibition of Tetraspanin Functions Impairs Human Papillomavirus and Cytomegalovirus Infections.International journal of molecular sciences · 2018Article
- Stabilization of the CD81 Large Extracellular Loop withPharmaceutics · 2018Article
- Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB.PLoS pathogens · 2018Article
- CD81 Receptor Regions outside the Large Extracellular Loop Determine Hepatitis C Virus Entry into Hepatoma Cells.Viruses · 2018Article
- Tspan2: a tetraspanin protein involved in oligodendrogenesis and cancer metastasis.Biochemical Society transactions · 2017Review
- The specificity of homomeric clustering of CD81 is mediated by its δ-loop.FEBS open bio · 2017Article
- TIMP-1 and CD82, a promising combined evaluation marker for PDAC.Oncotarget · 2017Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Hepatitis C virus (HCV) causes chronic liver disease, cirrhosis, and primary liver cancer. Despite 130 million people being at risk worldwide, no vaccine exists, and effective therapy is limited by drug resistance, toxicity, and high costs. The tetraspanin CD81 is an essential entry-level receptor required for HCV infection of hepatocytes and represents a critical target for intervention. In this study, we report the first structural characterization of the large extracellular loop of CD81, expressed in mammalian cells and studied in physiological solutions. The HCV E2 glycoprotein recognizes CD81 through a dynamic loop on the helical bundle, which was shown by nuclear magnetic resonance (NMR) spectroscopy to adopt a conformation distinct from that seen in crystals. A novel membrane binding interface was revealed adjacent to the exposed HCV interaction site in the extracellular loop of CD81. The binding pockets for two proposed inhibitors of the CD81-HCV interaction, namely, benzyl salicylate and fexofenadine, were shown to overlap the HCV and membrane interaction sites. Although the dynamic loop region targeted by these compounds presents challenges for structure-based design, the NMR assignments enable realistic screening and validation of ligands. Together, these data provide an improved avenue for developing potent agents that specifically block CD81-HCV interaction and also pave a way for elucidating the recognition mechanisms of diverse tetraspanins.
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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.