1. Amino- and carboxyl-terminal ends of the bovine parainfluenza virus type 3 matrix protein are important for virion and virus-like particle release.
- Author
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Ueda, Haruna, Yamakawa, Nagisa, and Takeuchi, Kaoru
- Subjects
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VIRUS-like particles , *PARAINFLUENZA viruses , *MEMBRANE transport proteins , *VIRION , *BOS - Abstract
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. [Display omitted] • M protein terminal ends are important for virion and VLP release. • M proteins without terminal ends were not transported. • The M protein YLDV sequence is critical for virion and VLP release. [ABSTRACT FROM AUTHOR]
- Published
- 2021
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