Paramyxovirus Phosphoproteins Form Homotrimers as Determined by an Epitope Dilution Assay, via Predicted Coiled Coils

• Published in: Virology (New York, N.Y.) Vol. 214; no. 1; pp. 139 - 149
• Main Authors: CURRAN, JOSEPH, BOECK, RONALD, LIN-MARQ, NATALIE, LUPAS, ANDREI, KOLAKOFSKY, DANIEL
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.12.1995
• Subjects: Amino Acid Sequence; Animals; Cell Line, Transformed; Epitopes; HeLa Cells; Humans; Molecular Sequence Data; Parainfluenza Virus 1, Human - metabolism; Phosphoproteins - chemistry; Phosphoproteins - metabolism; Protein Conformation; Sendai virus; Sequence Homology, Amino Acid; Transfection; Viral Proteins - chemistry; Viral Proteins - metabolism
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1995.9946

When HA epitope-tagged and untagged Sendai virus (SeV) P proteins are coexpressed and the products reacted with anti-HA, the untagged P protein is also selected because this protein is found as an oligomer. The oligomer was determined to be a homotrimer by coselection studies in which increasing amounts of untagged versus tagged protein were coexpressed, and these findings were extended to mumps virus, a member of therubulavirusgenus. The region of the SeV protein responsible for the oligomerization was localized to residues 344–411. Computer analysis of the 13ParamyxovirusP proteins in the database revealed that all but one are predicted to form coiled coils in this region, the first of only two regions that can be aligned throughout the entire virus subfamily. The predicted coiled-coil region of the measles virus P protein, when grafted onto the C-terminus of the normally monomeric La protein, led to the efficient oligomerization of this reporter protein. The predicted coiled-coil region of these P proteins thus appears to be sufficient for oligomerization.