ArticleJournal of virology2001
Role of the cytoplasmic domain of the beta-subunit of integrin alpha(v)beta6 in infection by foot-and-mouth disease virus.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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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Who cites it
20 citing papers in PubMed.
- Article
- Inhibition of viral replication by small interfering RNA targeting of the foot-and-mouth disease virus receptor integrin β6.Experimental and therapeutic medicine · 2017Article
- How foot-and-mouth disease virus receptor mediates foot-and-mouth disease virus infection.Virology journal · 2015Review
- Establishment and evaluation of a murine ανβ3-integrin-expressing cell line with increased susceptibility to Foot-and-mouth disease virus.Journal of veterinary science · 2015Article
- Article
- A dominant-negative mutant of rab5 inhibits infection of cells by foot-and-mouth disease virus: implications for virus entry.Journal of virology · 2009Article
- Heparan sulfate-binding foot-and-mouth disease virus enters cells via caveola-mediated endocytosis.Journal of virology · 2008Article
- Dendritic cell internalization of foot-and-mouth disease virus: influence of heparan sulfate binding on virus uptake and induction of the immune response.Journal of virology · 2008Article
- Specificity of the VP1 GH loop of Foot-and-Mouth Disease virus for alphav integrins.Journal of virology · 2006Article
- Early events in integrin alphavbeta6-mediated cell entry of foot-and-mouth disease virus.Journal of virology · 2005Article
- Analysis of foot-and-mouth disease virus internalization events in cultured cells.Journal of virology · 2005Article
- Acid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry.Journal of virology · 2005Article
- Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9.Journal of virology · 2004Article
- Integrin alphavbeta8 functions as a receptor for foot-and-mouth disease virus: role of the beta-chain cytodomain in integrin-mediated infection.Journal of virology · 2004Article
- Alteration of hepatitis A virus (HAV) particles by a soluble form of HAV cellular receptor 1 containing the immunoglobin-and mucin-like regions.Journal of virology · 2003Article
- Human rhinovirus type 2 is internalized by clathrin-mediated endocytosis.Journal of virology · 2003Article
- Foot-and-mouth disease virus receptors: comparison of bovine alpha(V) integrin utilization by type A and O viruses.Journal of virology · 2003Article
- Entry of viruses through the epithelial barrier: pathogenic trickery.Nature reviews. Molecular cell biology · 2003Review
- Heparan sulfate mediates infection of high-neurovirulence Theiler's viruses.Journal of virology · 2002Article
- Integrin alphavbeta1 is a receptor for foot-and-mouth disease virus.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Field isolates of foot-and-mouth disease virus (FMDV) are believed to use RGD-dependent integrins as cellular receptors in vivo. Using SW480 cell transfectants, we have recently established that one such integrin, alpha(v)beta6, functions as a receptor for FMDV. This integrin was shown to function as a receptor for virus attachment. However, it was not known if the alpha(v)beta6 receptor itself participated in the events that follow virus binding to the host cell. In the present study, we investigated the effects of various deletion mutations in the beta6 cytoplasmic domain on infection. Our results show that although loss of the beta6 cytoplasmic domain has little effect on virus binding, this domain is essential for infection, indicating a critical role in postattachment events. The importance of endosomal acidification in alpha(v)beta6-mediated infection was confirmed by experiments showing that infection could be blocked by concanamycin A, a specific inhibitor of the vacuolar ATPase.
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