Role of primary constitutive phosphorylation of Sendai virus P and V proteins in viral replication and pathogenesis.

Authors:
K Kiyotani
K Kiyotani
Hiroshima University School of Medicine
Japan
T Yoshida
T Yoshida
Finland; Helsinki Institute of Physics
Finland
Y Nagai
Y Nagai
University of Helsinki and Helsinki Institute of Physics
Finland

Virology 1999 Oct;263(1):195-208

Department of Immunology/Microbiology, Rush-Presbyterian-St. Luke's Medical Center, Chicago, Illinois 60612, USA.

Functional analysis of the primary constitutive phosphorylation of Sendai virus P and V proteins was performed using both in vitro and in vivo systems. Sendai virus minigenome transcription and replication in transfected cells were not significantly affected in the presence of primary phosphorylation deficient P protein (S249A, S249D, P250A) as measured by either the luciferase activity or the Northern blot analysis. Similarly, recombinant Sendai viruses lacking the primary phosphorylation in P grew to titers close to the wild-type virus in cell cultures and in the natural host of Sendai virus, the mouse. Mutant viruses showed no altered pathogenesis in mice lungs. Oligomerization of P by binding WT P or mutant P to GST-P (WT) Sepharose beads revealed that the primary phosphorylation was not crucial for P protein oligomerization. Similar to P protein primary phosphorylation, the V protein primary phosphorylation at serine249 was not essential for minigenome transcription and replication, as both WT and mutant V proteins were found equally inhibitory to the minigenome replication. These results show that the primary phosphorylation of P protein has no essential role in Sendai virus transcription, replication, and pathogenesis.

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http://dx.doi.org/10.1006/viro.1999.9953DOI Listing
October 1999
10 Citations
3.321 Impact Factor

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