Key result
Foot-and-mouth disease virus and its derived peptides form highly stable, EDTA-resistant complexes with the integrin αvβ6 receptor, which is dependent on specific leucine residues.
Population
RGD-containing peptides derived from the VP1 capsid protein of Foot-and-Mouth Disease Virus and FMDV…
Design
Preclinical
Authors
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May enhance FMDV infectivity via stable receptor binding in animals; leaves open leucine-targeted strategies pending in vivo validation.
The integrin-binding loop of FMDV forms highly stable, EDTA-resistant complexes with its principal receptor, integrin alphavbeta6, likely contributing to its high infectiousness.
DiCara et al. (2007) studied Foot-and-Mouth Disease Virus infection (in vitro). FMDV-derived peptides and virions vs. Control peptides / EDTA treatment was evaluated on EDTA-resistant binding to integrin αvβ6. Foot-and-mouth disease virus and its derived peptides form highly stable, EDTA-resistant complexes with the integrin αvβ6 receptor, which is dependent on specific leucine residues.
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