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Journal of Virology, October 2003, p. 10670-10676, Vol. 77, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.19.10670-10676.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Interaction between Human Respiratory Syncytial Virus (RSV) M2-1 and P Proteins Is Required for Reconstitution of M2-1-Dependent RSV Minigenome Activity

Stephen W. Mason,* Erika Aberg, Carol Lawetz, Rachel DeLong, Paul Whitehead, and Michel Liuzzi

Biological Sciences Department, Boehringer Ingelheim (Canada) Ltd., Laval, Québec, Canada

Received 25 March 2003/ Accepted 2 July 2003

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.

* Corresponding author. Mailing address: Boehringer Ingelheim (Canada) Ltd., Research & Development, 2100 rue Cunard, Laval, Québec H7S 2G5, Canada. Phone: (450) 682-4640. Fax: (450) 682-4642. E-mail: smason{at}lav.boehringer-ingelheim.com.

Journal of Virology, October 2003, p. 10670-10676, Vol. 77, No. 19
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.19.10670-10676.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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