Amino- and carboxyl-terminal ends of the bovine parainfluenza virus type 3 matrix protein are important for virion and virus-like particle release.

Paramyxovirus matrix (M) proteins are key drivers of virus particle assembly and budding at the plasma membrane. To identify regions important for the M protein function, we generated a series of deletion mutants of the bovine parainfluenza virus type 3 (BPIV3) M protein. We found that M proteins lacking 10 amino acids in the amino-terminal end (ΔN10) or 4 amino acids in the carboxyl-terminal end (ΔC4) did not support M-deficient BPIV3 virion release and M protein-induced virus-like particle (VLP) release. Both ΔN10 and ΔC4 retained M protein-M protein and M protein-nucleocapsid (N) protein interactions. However, neither was transported to the plasma membrane. Our results indicate that both amino- and carboxyl-terminal ends of the BPIV3 M protein are essential for M protein transport to the plasma membrane, where it facilitates virion and VLP release.