The Connector Domain of Vesicular Stomatitis Virus Large Protein Interacts with the Viral Phosphoprotein

Author:

Gould Joseph R.1,Qiu Shihong1,Shang Qiao1,Ogino Tomoaki2ORCID,Prevelige Peter E.1,Petit Chad M.3ORCID,Green Todd J.1

Affiliation:

1. Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA

2. Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA

3. Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA

Abstract

This study represents the first functional assignment of the connector domain of a Mononegavirales L protein. Furthermore, this study localizes P polymerase cofactor activity to specific amino acids. The functional necessity of this interaction, combined with the uniqueness of L and P proteins to the order Mononegavirales , makes disruption of the P-connector site a potential target for developing antivirals against other negative-strand RNA viruses. Furthermore, the connector domain as an acceptor site for the P protein represents a new understanding of Mononegavirales L protein biology.

Funder

HHS | NIH | National Cancer Institute

HHS | NIH | National Institute of Allergy and Infectious Diseases

HHS | NIH | National Center for Research Resources

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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