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MYH9 Aggregation Induced by Direct Interaction With PRRSV GP5 Ectodomain Facilitates Viral Internalization by

Biyun Xue1, Gaopeng Hou1, Guixi Zhang1

  • 1College of Veterinary Medicine, Northwest A&F University, Xianyang, China.

Frontiers in Microbiology
|October 26, 2019
PubMed

Insights

Porcine reproductive and respiratory syndrome virus (PRRSV) uses the MYH9 protein

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Mechanisms

Background:

  • Porcine reproductive and respiratory syndrome virus (PRRSV) infection control is hampered by incomplete knowledge of its invasion pathways.
  • Previous research identified an interaction between PRRSV glycoprotein GP5 and the MYH9 C-terminal domain protein (PRA).

Purpose of the Study:

  • To elucidate the specific interaction between PRRSV GP5 and MYH9 (PRA) and its role in viral entry.
  • To investigate the necessity of MYH9 filament assembly for PRRSV internalization.

Main Methods:

  • Investigated the interaction between PRRSV GP5 ectodomain 1 (GP5-ecto-1) and PRA.
  • Observed MYH9 filament assembly in transfected cells and PRRSV-infected cells (MARC-145 and porcine alveolar macrophages).
  • Assessed the impact of S100A4 (MYH9 disassembly inducer) on PRRSV infection.

Main Results:

  • GP5-ecto-1 directly binds PRA, initiating MYH9 filament assembly.
  • PRRSV infection induces endogenous MYH9 aggregation and polymerization, crucial for viral entry.
  • S100A4 overexpression reduced MYH9 aggregation and inhibited PRRSV-1 and PRRSV-2 internalization.

Conclusions:

  • MYH9 filament assembly is a novel molecular mechanism exploited by PRRSV for cell entry.
  • Targeting MYH9 polymerization presents a potential strategy for PRRSV prevention and control.
Keywords:
GP5MYH9PRRSVprotein–protein interactionvirus internalization

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