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Mapping and Functional Role of the Self-Association Domain of Vesicular Stomatitis Virus Phosphoprotein
- Source :
- Journal of Virology. 80:9511-9518
- Publication Year :
- 2006
- Publisher :
- American Society for Microbiology, 2006.
-
Abstract
- The phosphoprotein (P protein) of vesicular stomatitis virus (VSV) is an essential subunit of the viral RNA-dependent RNA polymerase complex and plays a central role in viral transcription and replication. Using both the yeast two-hybrid system and coimmunoprecipitation assays, we confirmed the self-association of the P protein of Indiana serotype (Pind) and heterotypic interaction between Pind and the P protein of New Jersey serotype (Pnj). Furthermore, by using various truncation and deletion mutants of Pind, the self-association domain of the Pind protein was mapped to amino acids 161 to 210 within the hinge region. The self-association domain of Pind protein is not required for its binding to nucleocapsid and large proteins. We further demonstrated that the self-association domain of Pind protein is essential for VSV transcription in a minireplicon system and that a synthetic peptide spanning amino acids 191 to 210 in the self-association domain of Pind protein strongly inhibited the transcription of the VSV genome in vitro in a dose-dependent manner. These results indicated that the self-association domain of Pind protein plays a critical role in VSV transcription.
- Subjects :
- Transcription, Genetic
Immunoprecipitation
viruses
Protein subunit
Molecular Sequence Data
Immunology
Genome, Viral
Saccharomyces cerevisiae
Peptide Mapping
Microbiology
Vesicular stomatitis Indiana virus
Cell Line
Transcription (biology)
Cricetinae
Two-Hybrid System Techniques
Virology
Animals
Humans
Amino Acid Sequence
RNA, Messenger
Peptide sequence
biology
Structure and Assembly
RNA
Vesiculovirus
Rhabdoviridae
Phosphoproteins
biology.organism_classification
Molecular biology
Vesicular stomatitis virus
Insect Science
Phosphoprotein
Mutation
Protein Binding
Subjects
Details
- ISSN :
- 10985514 and 0022538X
- Volume :
- 80
- Database :
- OpenAIRE
- Journal :
- Journal of Virology
- Accession number :
- edsair.doi.dedup.....5b3ce7d7313365980d4f8ba2fff0231b