Role of palmitoylation of membrane protein CM2 in influenza C virus replication

摘要

CM2 is the second membrane protein of influenza C virus and is posttranslationally modified by phosphorylation, palmitoylation, N-glycosylation, and dimer/tetramer formation. In the present study, we generated rCM2-C65A, a recombinant influenza C virus lacking CM2 palmitoylation site, and examined viral growth and viral protein synthesis in the recombinant-infected cells. The rCM2-C65A virus grew less efficiently than did the wild-type virus. Membrane flotation analysis of the infected cells revealed that less NP was recovered in the plasma membrane fractions of the rCM2-C65A-infected cells than that in the wild-type virus-infected cells, suggesting that palmitoylation of CM2 is involved in the affinity of the ribonucleoprotein complex to the plasma membrane, leading to the efficient generation of infectious viruses.