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Journal of Virology, January 1999, p. 242-250, Vol. 73, No. 1
Department of Clinical Virology, Federal
Research Centre for Virus Diseases of Animals, D-72076
Tübingen, Germany
Received 10 June 1998/Accepted 18 September 1998
To elucidate the functions of rhabdovirus matrix (M) protein, we
determined the localization of M in rabies virus (RV) and analyzed the
properties of an M-deficient RV mutant. We provide evidence that M
completely covers the ribonucleoprotein (RNP) coil and keeps it in a
condensed form. As determined by cosedimentation experiments, not only
the M-RNP complex but also M alone was found to interact specifically
with the glycoprotein G. In contrast, an interaction of G with
the nucleoprotein N or M-less RNP was not observed. In the absence of
M, infectious particles were mainly cell associated and the yield of
cell-free infectious virus was reduced by as much as 500,000-fold,
demonstrating the crucial role of M in virus budding. Supernatants from
cells infected with the M-deficient RV did not contain the typical
bullet-shaped rhabdovirus particles but instead contained long,
rod-shaped virions, demonstrating severe impairment of the virus
formation process. Complementation with M protein expressed from
plasmids rescued rhabdovirus formation. These results
demonstrate the pivotal role of M protein in condensing and
targeting the RNP to the plasma membrane as well as in incorporation of
G protein into budding virions.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Matrix Protein of Rabies Virus Is Responsible for the Assembly
and Budding of Bullet-Shaped Particles and Interacts with the
Transmembrane Spike Glycoprotein G

*
Corresponding author. Mailing address: Federal Research
Centre for Virus Diseases of Animals, Paul-Ehrlich-Strasse 28, D-72076 Tübingen, Germany. Phone: 49 7071 967 205. Fax: 49 7071 967303. E-mail: conzelmann{at}tue.bfav.de.
Present address: Intervet International b.v., NL-5830 AA
Boxmeer, The Netherlands.
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