Interaction between human respiratory syncytial virus (RSV) M2-1 and P proteins is required for reconstitution of M2-1-dependent RSV minigenome activity.
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.
Mason
Stephen W
SW
Biological Sciences Department, Boehringer Ingelheim (Canada) Ltd, Laval, Québec, Canada. smason@lav.boehringer-ingelheim.com
Aberg
Erika
E
Lawetz
Carol
C
DeLong
Rachel
R
Whitehead
Paul
P
Liuzzi
Michel
M
D002846:Chromatography, Affinity; D016679:Genome, Viral; D006801:Humans; D010766:Phosphorylation; D018113:Respiratory Syncytial Virus, Human / Q000235:genetics*; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology*; D014779:Virus Replication
D014764:Viral Proteins