ArticleJournal of virology2004
Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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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Who cites it
52 citing papers in PubMed, 103 citations in OpenAlex.
- Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection.Nature communications · 2025Article
- Establishment of a Panel of Human Cell Lines to Identify Cellular Receptors Used byInternational journal of molecular sciences · 2025Article
- Receptors and Host Factors for Enterovirus Infection: Implications for Cancer Therapy.Cancers · 2024Review
- The early communication stages between serine proteases and enterovirus capsids in the race for viral disintegration.Communications biology · 2024Article
- A Receptor Integrin β1 Promotes Infection of Avian Metapneumovirus Subgroup C by Recognizing a Viral Fusion Protein RSD Motif.International journal of molecular sciences · 2024Article
- Pathogenesis of enterovirus infection in central nervous system.Biosafety and health · 2023Review
- Molecular mimicry of host short linear motif-mediated interactions utilised by viruses for entry.Molecular biology reports · 2023Review
- Recombinant Viral Vectors for Therapeutic Programming of Tumour Microenvironment: Advantages and Limitations.Biomedicines · 2022Review
- Integrin mediates cell entry of the SARS-CoV-2 virus independent of cellular receptor ACE2.The Journal of biological chemistry · 2022Article
- The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection.PLoS pathogens · 2021Article
- The Enterovirus Theory of Disease Etiology in Myalgic Encephalomyelitis/Chronic Fatigue Syndrome: A Critical Review.Frontiers in medicine · 2021Review
- Article
- Why COVID-19 Transmission Is More Efficient and Aggressive Than Viral Transmission in Previous Coronavirus Epidemics?Biomolecules · 2020Review
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- A potential role for integrins in host cell entry by SARS-CoV-2.Antiviral research · 2020Article
- Recombination Events and Conserved Nature of Receptor Binding Motifs in Coxsackievirus A9 Isolates.Viruses · 2020Article
- Article
- Evolutionary and Structural Overview of Human Picornavirus Capsid Antibody Evasion.Frontiers in cellular and infection microbiology · 2019Review
- The life cycle of non-polio enteroviruses and how to target it.Nature reviews. Microbiology · 2018Review
- Integrins are not essential for entry of coxsackievirus A9 into SW480 human colon adenocarcinoma cells.Virology journal · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
Coxsackievirus A9 (CAV9), a member of the Enterovirus genus of Picornaviridae, is a common human pathogen and is one of a significant number of viruses containing a functional arginine-glycine-aspartic acid (RGD) motif in one of their capsid proteins. Previous studies identified the RGD-recognizing integrin alpha(v)beta(3) as its cellular receptor. However, integrin alpha(v)beta(6) has been shown to be an efficient receptor for another RGD-containing picornavirus, foot-and-mouth disease virus (FMDV). In view of the similarity in sequence context of the RGD motifs in CAV9 and FMDV, we investigated whether alpha(v)beta(6) can also serve as a receptor for CAV9. We found that CAV9 can bind to purified alpha(v)beta(6) and also to SW480 cells transfected with beta(6) cDNA, allowing expression of alpha(v)beta(6) on their surface, but it cannot bind to mock-transfected cells. In addition, a higher yield of CAV9 was obtained in beta(6)-expressing cells than in mock-transfected cells. There was no similar enhancement in infection with an RGD-less CAV9 mutant. We also found beta(6) on the surface of GMK cells, a cell line which CAV9 infects efficiently by an RGD-dependent mechanism. Significantly, this infection is blocked by an antibody to alpha(v)beta(6), while this antibody did not block the low level of infection by the RGD-less mutant. Thus, integrin alpha(v)beta(6) is an RGD-dependent receptor for CAV9 and may be important in natural CAV9 infections.
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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.