Journal of Virology, January 2001, p. 527-532, Vol. 75, No. 1
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.1.527-532.2001
v
3 To Function as a Receptor for
Foot-and-Mouth Disease Virus Is Not Dependent on the Presence of
Complete Subunit Cytoplasmic Domains
Foot-and-Mouth Disease Research Unit, United States Department of Agriculture, Agricultural Research Service, Plum Island Animal Disease Center, Greenport, New York 11944
Received 26 April 2000/Accepted 29 September 2000
The integrin
v
3 has been shown to
function as one of the integrin receptors on cultured cells for
foot-and-mouth disease virus (FMDV), and high-efficiency utilization of
the bovine homolog of this integrin is dependent on the cysteine-rich
repeat region of the bovine
3 subunit. In this study we
have examined the role of the cytoplasmic domains of the
v and
3 subunits in FMDV infection. We
have found that truncations or extensions of these domains of either
subunit, including deletions removing almost all of the cytoplasmic
domains, had little or no effect on the ability of the integrin to
function as a receptor for FMDV. The lysosomotropic agent monensin
inhibited viral replication in cells transfected with either intact or
cytoplasmic domain-truncated
v
3. In
addition, viral replication in transfected cells was inhibited by an
v
3 function-blocking antibody but not by
function-blocking antibodies to three other RGD-directed integrins,
suggesting that these integrins are not involved in the infectious
process. These results indicate that alterations to the cytoplasmic
domains of either subunit, which lead to the inability of the integrin
receptor to function normally, do not abolish the ability of the
integrin to bind and internalize this viral ligand.
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