TY - JOUR
T1 - Characterization of a membrane-associated protein implicated in visna virus binding and infection
AU - Bruett, Linda
AU - Barber, Sheila A.
AU - Clements, Janice E.
N1 - Funding Information:
The authors thank Dr. Barry Margulies for helpful discussions, Debbie Hauer and David Herbst for excellent technical support, Dr. Deborah McClellan for editorial suggestions, and Maryann Brooks for her help in preparing the manuscript. This work was supported by NIH Grants NSO7392 and NS23039.
PY - 2000/5/25
Y1 - 2000/5/25
N2 - The identity of the cellular receptor(s) for visna virus, an ovine lentivirus, is currently unknown; however, previous studies from our laboratory have identified membrane-associated proteins expressed selectively in susceptible cells which bind visna virus. Moreover, a polyclonal antibody (2-23), raised against a 45-kDa visna virus binding protein, bound specifically to the surface of susceptible cells in immunofluorescence assays and significantly reduced binding of visna virus to cells (S. E. Crane et al., 1991, J. Virol., 65, 6137-6143). In this report we extend our studies of this antibody (2-23), showing both that 2-23 significantly reducers visna virus infection of susceptible cells and that 2-23 immunoprecipitates a putative protein complex consisting of a prominent 30-kDa protein, as well as the 45-kDa immunogen, specifically from radiolabeled virus-susceptible sheep cells. Further, we demonstrate that the 30-kDa protein is a membrane- associated proteoglycan substituted with a chondroitin sulfate glycosaminoglycan (GAG) chain(s) and that treatment of susceptible cells with an inhibitor of GAG synthesis significantly reduces visna virus production. Collectively, these data support a role for a proteoglycan in visna virus cell binding and infection.
AB - The identity of the cellular receptor(s) for visna virus, an ovine lentivirus, is currently unknown; however, previous studies from our laboratory have identified membrane-associated proteins expressed selectively in susceptible cells which bind visna virus. Moreover, a polyclonal antibody (2-23), raised against a 45-kDa visna virus binding protein, bound specifically to the surface of susceptible cells in immunofluorescence assays and significantly reduced binding of visna virus to cells (S. E. Crane et al., 1991, J. Virol., 65, 6137-6143). In this report we extend our studies of this antibody (2-23), showing both that 2-23 significantly reducers visna virus infection of susceptible cells and that 2-23 immunoprecipitates a putative protein complex consisting of a prominent 30-kDa protein, as well as the 45-kDa immunogen, specifically from radiolabeled virus-susceptible sheep cells. Further, we demonstrate that the 30-kDa protein is a membrane- associated proteoglycan substituted with a chondroitin sulfate glycosaminoglycan (GAG) chain(s) and that treatment of susceptible cells with an inhibitor of GAG synthesis significantly reduces visna virus production. Collectively, these data support a role for a proteoglycan in visna virus cell binding and infection.
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U2 - 10.1006/viro.2000.0309
DO - 10.1006/viro.2000.0309
M3 - Article
C2 - 10814578
AN - SCOPUS:0034713441
SN - 0042-6822
VL - 271
SP - 132
EP - 141
JO - Virology
JF - Virology
IS - 1
ER -