ArticleJournal of virology2003
Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 56 citations in OpenAlex.
- Polyomavirus Wakes Up and Chooses Neurovirulence.Viruses · 2023Review
- Sending mixed signals: polyomavirus entry and trafficking.Current opinion in virology · 2021Review
- Taking the Scenic Route: Polyomaviruses Utilize Multiple Pathways to Reach the Same Destination.Viruses · 2020Review
- Microtubules in Polyomavirus Infection.Viruses · 2020Review
- Chrysin Attenuates VCAM-1 Expression and Monocyte Adhesion in Lipopolysaccharide-Stimulated Brain Endothelial Cells by Preventing NF-κB Signaling.International journal of molecular sciences · 2017Article
- Article
- Different applications of virus-like particles in biology and medicine: Vaccination and delivery systems.Biopolymers · 2016Review
- Beyond RGD: virus interactions with integrins.Archives of virology · 2015Review
- Ganglioside and Non-ganglioside Mediated Host Responses to the Mouse Polyomavirus.PLoS pathogens · 2015Article
- Sialic Acid Receptors of Viruses.Topics in current chemistry · 2015Review
- Nanoscale assemblies and their biomedical applications.Journal of the Royal Society, Interface · 2013Review
- Amino Acid Sequences Mediating Vascular Cell Adhesion Molecule 1 Binding to Integrin Alpha 4: Homologous DSP Sequence Found for JC Polyoma VP1 Coat Protein.Neurology international · 2013Article
- Lipids and proteins act in opposing manners to regulate polyomavirus infection.Journal of virology · 2010Article
- Article
- The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry.Virology · 2009Review
- Identification and characterization of an antigen I/II family protein produced by group A Streptococcus.Infection and immunity · 2006Article
- Mouse polyomavirus enters early endosomes, requires their acidic pH for productive infection, and meets transferrin cargo in Rab11-positive endosomes.Journal of virology · 2006Article
- The role of sialic acid in human polyomavirus infections.Glycoconjugate journal · 2006Review
- Establishment of an immunoscreening system using recombinant VP1 protein for the isolation of a monoclonal antibody that blocks JC virus infection.Biochemical and biophysical research communications · 2005Article
- Uptake pathway of polyomavirus via ganglioside GD1a.Journal of virology · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The initial interaction of murine polyomavirus (Py) with host cells occurs through direct binding of the major capsid protein VP1 with cell membrane molecules containing terminal sialic acids; however, these Py receptor molecules have not yet been identified. Analysis of the capsid protein primary sequences of all murine strains revealed the presence of integrin ligand motifs in the DE and EF loops of VP1 (LDV and DLXXL, respectively) and at the N terminus of VP2 (DGE). We show that infectivity of the Py A2 strain in mouse Swiss 3T3 fibroblasts is significantly reduced only in the presence of natural integrin ligands carrying an LDV motif or antibodies directed against the alpha4 and beta1 integrin subunits. Furthermore, we demonstrate that expression of the alpha4 subunit in the alpha4-deficient BALB/c 3T3 cells increases viral infectivity. Addition of alpha4 function-blocking antibodies, prior to or after virus adsorption, blocks this increased infectivity without affecting virus binding to cells. Taken together, these data indicate that expression of alpha4 integrin enhances permissivity to Py, probably by acting as one of the postattachment receptors.
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.