Work

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

Year: 2020

Type: article

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.

Source: Journal of Virology

DOI: 10.1128/jvi.01729-19

Authors: Joseph R. Gould, Shihong Qiu, Qiao Shang, Tomoaki Ogino, Peter E. Prevelige, Chad M. Petit, Todd J. Green

Institutions: University of Alabama at Birmingham, Case Western Reserve University

Language: English

Topic: Virology and Viral Diseases

Subfield: Epidemiology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Cancer Institute, National Institute of Allergy and Infectious Diseases, National Center for Research Resources

Awards: Dissecting catalytic and regulatory functions of nonsegmented negative strandRNA viral polymerases, G411786793, G450836581, G479545533, Strain Dependent Structure and Function of the Influenza NS1 Protein, 800 MHz NMR Spectrometer for the Central Alabama High-Field NMR Facility, Transcription and replication in nonsegmented negative-strand RNA viruses, Comprehensive Cancer Center Support Grant

OpenAlex ID: W2997509228

FWCI: 1.611

Cites: 51

Cited by: 13

Related to: 10