ArticleJournal of virology2010
Interaction of alphaVbeta3 and alphaVbeta6 integrins with human parechovirus 1.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed.
- Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection.Nature communications · 2025Article
- Review
- MYADM binds human parechovirus 1 and is essential for viral entry.Nature communications · 2024Article
- Myeloid-associated differentiation marker is an essential host factor for human parechovirus PeV-A3 entry.Nature communications · 2023Article
- The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection.PLoS pathogens · 2021Article
- A comparative analysis of parechovirus protein structures with other picornaviruses.Open biology · 2021Article
- Article
- Assembly of infectious enteroviruses depends on multiple, conserved genomic RNA-coat protein contacts.PLoS pathogens · 2020Article
- RNA-Mediated Virus Assembly: Mechanisms and Consequences for Viral Evolution and Therapy.Annual review of biophysics · 2019Review
- A 2.8-Angstrom-Resolution Cryo-Electron Microscopy Structure of Human Parechovirus 3 in Complex with Fab from a Neutralizing Antibody.Journal of virology · 2019Article
- Human Parechovirus 1, 3 and 4 Neutralizing Antibodies in Dutch Mothers and Infants and Their Role in Protection Against Disease.The Pediatric infectious disease journal · 2018Article
- Polarized Entry of Human Parechoviruses in the Airway Epithelium.Frontiers in cellular and infection microbiology · 2018Article
- Human Parechovirus: an Increasingly Recognized Cause of Sepsis-Like Illness in Young Infants.Clinical microbiology reviews · 2018Review
- Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus.Nature communications · 2017Article
- Genomic RNA folding mediates assembly of human parechovirus.Nature communications · 2017Article
- Multiple capsid-stabilizing interactions revealed in a high-resolution structure of an emerging picornavirus causing neonatal sepsis.Nature communications · 2016Article
- The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid.Journal of virology · 2016Article
- Human Parechovirus 1 Infection Occurs via αVβ1 Integrin.PloS one · 2016Article
- Role of Heparan Sulfate in Cellular Infection of Integrin-Binding Coxsackievirus A9 and Human Parechovirus 1 Isolates.PloS one · 2016Article
- Structure of Ljungan virus provides insight into genome packaging of this picornavirus.Nature communications · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Human parechovirus (HPEV) infections are very common in early childhood and can be severe in neonates. It has been shown that integrins are important for cellular infectivity of HPEV1 through experiments using peptide blocking assays and function-blocking antibodies to alpha(V) integrins. The interaction of HPEV1 with alpha(V) integrins is presumably mediated by a C-terminal RGD motif in the capsid protein VP1. We characterized the binding of integrins alpha(V)beta(3) and alpha(V)beta(6) to HPEV1 by biochemical and structural studies. We showed that although HPEV1 bound efficiently to immobilized integrins, alpha(V)beta(6) bound more efficiently than alpha(V)beta(3) to immobilized HPEV1. Moreover, soluble alpha(V)beta(6), but not alpha(V)beta(3), blocked HPEV1 cellular infectivity, indicating that it is a high-affinity receptor for HPEV1. We also showed that HPEV1 binding to integrins in vitro could be partially blocked by RGD peptides. Using electron cryo-microscopy and image reconstruction, we showed that HPEV1 has the typical T=1 (pseudo T=3) organization of a picornavirus. Complexes of HPEV1 and integrins indicated that both integrin footprints reside between the 5-fold and 3-fold symmetry axes. This result does not match the RGD position predicted from the coxsackievirus A9 X-ray structure but is consistent with the predicted location of this motif in the shorter C terminus found in HPEV1. This first structural characterization of a parechovirus indicates that the differences in receptor binding are due to the amino acid differences in the integrins rather than to significantly different viral footprints.
Indexed as
Identifiers
What OpenQuestion holds
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.