Work

Mapping and Functional Role of the Self-Association Domain of Vesicular Stomatitis Virus Phosphoprotein

Year: 2006

Type: article

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.

Source: Journal of Virology

DOI: 10.1128/jvi.01035-06

Authors: Mingzhou Chen, Tomoaki Ogino, Amiya K. Banerjee

Institutions: Cleveland Clinic, Cleveland Clinic Research

Language: English

Topic: Virology and Viral Diseases

Subfield: Epidemiology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funder: National Institute of Allergy and Infectious Diseases

Awards: G1450119653, Gene Expression of Negative strand RNA Viruses