Interaction Between Human Respiratory Syncytial Virus (RSV) M2-1 and P Proteins is Required for Reconstitution of M2-1-dependent RSV Minigenome Activity

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2003 Sep 13

PMID 12970453

Citations 36

Authors

Stephen W Mason

Erika Aberg

Carol Lawetz

Rachel DeLong

Paul Whitehead

Michel Liuzzi

Affiliations

Soon will be listed here.

Abstract

We have investigated protein-protein interactions among the respiratory syncytial virus (RSV) RNA polymerase subunits using affinity chromatography. Here we demonstrate a novel interaction of P and M2-1 proteins. Phosphorylation of either M2-1 or P appears to be dispensable for this interaction. Internal deletions within P mapped the M2-1-binding domain to a region between residues 100 and 120. Alanine-scanning mutagenesis within this region of P revealed that substitution of any one of the three residues, L101, Y102, and F109, prevented both M2-1 and P binding and expression of an M2-1-dependent luciferase reporter gene. However, these same mutations did not prevent the activity of an M2-1-independent chloramphenicol acetyltransferase minigenome, suggesting that these residues of P specifically affect M2-1-P interaction. On the basis of these observations, it is possible that the interaction between RSV M2-1 and P proteins is important for viral replication.

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