R. Melki et al., INTERACTION BETWEEN TUBULIN AND THE VIRAL MATRIX PROTEIN OF VESICULARSTOMATITIS-VIRUS - POSSIBLE IMPLICATIONS IN THE VIRAL CYTOPATHIC EFFECT, Virology, 202(1), 1994, pp. 339-347
The matrix (M) protein of vesicular stomatitis virus has been shown to
induce the rounding of cells. Experiments were performed in order to
define the mechanism by which M protein could cause this cytopathic ef
fect (CPE). Immunofluorescence experiments performed on infected cells
indicate that cellular rounding coincides with the disruption of the
microtubular network. Immunoprecipitation of M protein or tubulin in i
nfected cell extract demonstrates an association of these two proteins
in vivo. We show that M protein is capable of interacting in vitro wi
th tubulin in both its polymerized and nonassembled forms. Studies usi
ng proteolytically cleaved proteins indicate that this interaction occ
urs via the highly basic N-terminal domain of M protein and the highly
acidic C-terminal region of tubulin. Furthermore, a thermosensitive m
utant (tsG33) containing a mutation in the matrix protein gene which i
s unable to induce CPE at nonpermissive temperature interacts with tub
ulin with a lower affinity. These results demonstrate that M protein i
nteracts with tubulin in vivo and in vitro and strongly suggest that C
PE is caused by this interaction. (C) 1994 academic Press, Inc.