ArticleJournal of virology2012
Symmetry-related clustering of positive charges is a common mechanism for heparan sulfate binding in enteroviruses.
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 22 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.
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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
22 citing papers in PubMed, 33 citations in OpenAlex.
- Nondestructive tracking of viral infections by viral protein-initiated fluorescent sensors.Journal of virology · 2026Article
- Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism.Viruses · 2024Review
- Review
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- Antivirals blocking entry of enteroviruses and therapeutic potential.Journal of biomedical science · 2021Review
- Symmetrical arrangement of positively charged residues around the 5-fold axes of SAT type foot-and-mouth disease virus enhances cell culture of field viruses.PLoS pathogens · 2020Article
- Cellular receptors for enterovirus A71.Journal of biomedical science · 2020Review
- Recombination Events and Conserved Nature of Receptor Binding Motifs in Coxsackievirus A9 Isolates.Viruses · 2020Article
- Evolutionary and Structural Overview of Human Picornavirus Capsid Antibody Evasion.Frontiers in cellular and infection microbiology · 2019Review
- Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor.Emerging microbes & infections · 2017Article
- Suramin interacts with the positively charged region surrounding the 5-fold axis of the EV-A71 capsid and inhibits multiple enterovirus A.Scientific reports · 2017Article
- Role of Heparan Sulfate in Cellular Infection of Integrin-Binding Coxsackievirus A9 and Human Parechovirus 1 Isolates.PloS one · 2016Article
- Single Neutralizing Monoclonal Antibodies Targeting the VP1 GH Loop of Enterovirus 71 Inhibit both Virus Attachment and Internalization during Viral Entry.Journal of virology · 2015Article
- A small molecule inhibits virion attachment to heparan sulfate- or sialic acid-containing glycans.Journal of virology · 2014Article
- Initial evidence on differences among Enterovirus 71, Coxsackievirus A16 and Coxsackievirus B4 in binding to cell surface heparan sulphate.Virusdisease · 2014Article
- Human astrocytic cells support persistent coxsackievirus B3 infection.Journal of virology · 2013Article
- A strain-specific epitope of enterovirus 71 identified by cryo-electron microscopy of the complex with fab from neutralizing antibody.Journal of virology · 2013Article
- Positively charged residues at the five-fold symmetry axis of cell culture-adapted foot-and-mouth disease virus permit novel receptor interactions.Journal of virology · 2013Article
- Structures of the procapsid and mature virion of enterovirus 71 strain 1095.Journal of virology · 2013Article
- Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxsackievirus A9 (CAV9), a member of the Picornaviridae family, uses an RGD motif in the VP1 capsid protein to bind to integrin αvβ6 during cell entry. Here we report that two CAV9 isolates can bind to the heparan sulfate/heparin class of proteoglycans (HSPG). Sequence analysis identified an arginine (R) at position 132 in VP1 in these two isolates, rather than a threonine (T) as seen in the nonbinding strains tested. We introduced a T132R substitution into the HSPG-nonbinding strain Griggs and recovered infectious virus capable of binding to immobilized heparin, unlike the parental Griggs strain. The known CAV9 structure was used to identify the location of VP1 position 132, 5 copies of which were found to cluster around the 5-fold axis of symmetry, presumably producing a region of positive charge which can interact with the negatively charged HSPG. Analysis of several enteroviruses of the same species as CAV9, Human enterovirus B (HEV-B), identified examples from 5 types in which blocking of infection by heparin was coincident with an arginine (or another basic amino acid, lysine) at a position corresponding to 132 in VP1 in CAV9. Together, these data show that membrane-associated HSPG can serve as a (co)receptor for some CAV9 and other HEV-B strains and identify symmetry-related clustering of positive charges as one mechanism by which HSPG binding can be achieved. This is a potentially powerful mechanism by which a single amino acid change could generate novel receptor binding capabilities, underscoring the plasticity of host-cell interactions in enteroviruses.
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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.