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Journal of Virology, February 1999, p. 1661-1664, Vol. 73, No. 2
Department of Microbiology and Immunology,
Thomas Jefferson University, Philadelphia, Pennsylvania 19107
Received 31 July 1998/Accepted 21 October 1998
One of the major structural differences between rabies virus and
vesicular stomatitis virus (VSV) is that the nucleoprotein (N) is the
major phosphoprotein and the nominal phosphoprotein (P) is less
phosphorylated in rabies virus, whereas P is the major phosphoprotein
and N is not phosphorylated in VSV. We investigated the function of
phosphorylation of rabies virus N after dephosphorylation of N with
alkaline phosphatase or after changing the phosphorylated serine at
position 389 to alanine by site-directed mutagenesis. The
unphosphorylated N, in comparison to the phosphorylated N, was studied
for its abilities to encapsidate rabies virus leader RNA and to support
transcription and replication of a rabies virus minigenome. We found
that unphosphorylated N binds more strongly to leader RNA than the
phosphorylated N; however, the rates of transcription and replication
of the rabies virus minigenome were significantly lower with the
unphosphorylated N than with the phosphorylated N. This indicates that
the phosphorylation of rabies virus N plays an important role in the
regulation of rabies virus transcription and replication, probably via
modulation of leader RNA encapsidation.
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Phosphorylation of Rabies Virus Nucleoprotein
Regulates Viral RNA Transcription and Replication by Modulating Leader
RNA Encapsidation
*
Corresponding author. Present address: Department of
Diagnostic Medicine and Pathobiology, School of Veterinary Medicine, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506. Phone:
(785) 532-4407. Fax: (785) 532-4481. E-mail:
zhenfu{at}vet.ksu.edu.
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