Jh. Broughan et Wh. Wunner, CHARACTERIZATION OF PROTEIN INVOLVEMENT IN RABIES VIRUS BINDING TO BHK-21-CELLS, Archives of virology, 140(1), 1995, pp. 75-93
Prior studies established the specificity of rabies virus receptors on
BHK-21 cells based on the saturability of the receptors and on compet
itive binding. In the present study, we used protease-treated cells to
identify the involvement of protein in the specific binding of rabies
virus to these cells. In addition, biochemical characterization of n-
octylglucoside solubilized BHK-21 plasma membranes demonstrated the in
volvement of a protease sensitive, heat insensitive, integral membrane
protein or protein complex in rabies virus binding to these cells. Th
e membrane component that binds rabies virus is associated with a high
molecular weight fraction of the n-octylglucoside-plasma membrane ext
ract isolated by gel filtration. This high molecular weight fraction (
similar to 450 KDa) is enriched with a cell surface integral membrane
component that comigrates with denatured bovine serum fibronectin (220
KDa). This cellular component did not bind polyclonal antisera to fib
ronectin in Western blot (native or denatured) or immunoprecipitation
experiments. Direct and specific virus binding to high molecular weigh
t plasma membrane protein(s) separated on Western blots further confir
med the role of a protein receptor in rabies virus binding to these ce
lls.