Abstract
The mechanism by which the foot-and-mouth disease virus (FMDV) initiates infection of cells is thought to involve the attachment of the viral capsid to host integrins on the surface of target cells. However, the role of integrins in FMDV infection still needs to be fully understood, although it has been demonstrated that integrin αvβ6 interferes with FMDV in vitro and results in neutralization of its infectivity. In the present study, we describe the cloning and sequencing of suckling mouse integrin β6 and the subsequent expression of two segments of integrin β6 extracellular domains: β6-1 (which contains the ligand-binding domain) and β6-2. Sequencing of the mouse integrin β6 subunit revealed close homology (~90%) with its human counterpart. When recombinant integrin extracellular domains β6-1 and β6-2 formulated with adjuvant were inoculated into guinea pigs, anti-integrin antibody expression was high before FMDV challenge. Interestingly, guinea pigs (50%) inoculated with integrin β6-1 were protected from FMDV infection; in contrast, none of the animals inoculated with integrin β6-2 were protected. This result indicates that an integrin blockade may be able to interfere with FMDV infection in vivo, which raises the possibility that targeting integrin in vivo may be the basis for a new strategy to control FMDV infection.
Highlights
Foot-and-mouth disease (FMD) is one of the most economically devastating diseases that affects a large number of cloven-hoofed animals, including cattle, pigs, sheep, goats, and camels [1,2]
The mechanism by which foot-and-mouth disease virus (FMDV) initiates infection of cells is thought to involve the attachment of the viral capsid to host integrins on the surface of target cells [4,5]
We have investigated the role of integrin β6 extracellular domains β6-1 and β6-2 in the neutralization of FMDV infection in vitro in CHO-K1-αvβ6 cells and in vivo in guinea pigs
Summary
Foot-and-mouth disease (FMD) is one of the most economically devastating diseases that affects a large number of cloven-hoofed animals, including cattle, pigs, sheep, goats, and camels [1,2]. On investigating the mechanism for αvβ6-mediated infection, it was found that loss of the β6 cytoplasmic domain of the integrin has little effect on the binding of virus to cells [20]. The mechanism is likely to involve inhibition of the binding of the virus to cells via binding of integrin to the receptor-binding site on the virus This result indicates that interference with αvβ can neutralize virus infection in vivo. Inhibition of the binding of virus to cells via RGD-binding integrins has been invaluable for the study of viral infections, but there have been no studies on the impact of αvβ6-mediated neutralization of FMDV infection in vivo. We found that the β6-1 segment provided guinea pigs with partial protection against the FMDV challenge This is a promising result based on which new strategies to control FMDV infection in vivo can be established
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
