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

Virology. 2021 Sep:561:17-27. doi: 10.1016/j.virol.2021.05.014. Epub 2021 Jun 6.

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.

Keywords: Bovine parainfluenza virus type 3; M protein; Virus budding; Virus-like particle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane / metabolism
  • Chlorocebus aethiops
  • Mutant Proteins / metabolism
  • Nucleocapsid Proteins / metabolism
  • Parainfluenza Virus 3, Bovine / chemistry
  • Parainfluenza Virus 3, Bovine / physiology*
  • Protein Transport
  • Sequence Deletion
  • Vero Cells
  • Viral Matrix Proteins / chemistry*
  • Viral Matrix Proteins / genetics
  • Viral Matrix Proteins / metabolism*
  • Virion / physiology*
  • Virus Release*

Substances

  • Mutant Proteins
  • Nucleocapsid Proteins
  • Viral Matrix Proteins