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Identification of MYH9 Key Domain Involved in the Entry of PRRSV Into Permissive Cells
Liangliang Li1, Weiyao Sun2, Qifan Hu2
1College of Agronomy, Liaocheng University, Liaocheng, China.
Abstract:
Porcine reproductive and respiratory syndrome virus (PRRSV) is an important pathogen that causes huge losses economically to the pig industry worldwide. Previous research suggested that receptor dependence is necessary for PRRSV infection. MYH9 and CD163 are indispensable for PRRSV entry into a porcine alveolar macrophage. In the present study, human MYH9 (hMYH9) and mouse MYH9 (mMYH9), similar to swine MYH9, could also accelerate PRRSV infection in pCD163-mediated cell lines. Knockdown of MYH9 activity using the specific small interfering RNA or inhibitor (blebbistatin) concomitantly decreased PRRSV infection. C-terminal fragment of MYH9 (PRA) proteins from different mammalian species contains a conserved binding domain (aa1676-1791) for PRRSV binding, since the recombinant MYH91676-1791protein could inhibit the PRRSV infection significantly. Furthermore, the specific polyclonal antibody of MYH91676-1791 could block PRRSV infection in host cells. These data strongly supported that MYH9, a very important cofactor, participated in PRRSV entry into target cells, which may facilitate the development of a new therapeutic agent to control PRRSV infection.
Insights
Myosin IIA (MYH9) is crucial for Porcine reproductive and respiratory syndrome virus (PRRSV) entry into host cells. Inhibiting MYH9 significantly reduces PRRSV infection, offering new therapeutic targets.
Area of Science:
- Veterinary Virology
- Molecular Biology
- Cellular Biology
Background:
- Porcine reproductive and respiratory syndrome virus (PRRSV) causes significant economic losses in the global swine industry.
- PRRSV infection is dependent on specific cellular receptors, with MYH9 and CD163 identified as essential for entry into porcine alveolar macrophages.
Purpose of the Study:
- To investigate the role of Myosin IIA (MYH9) as a cofactor in PRRSV entry into host cells.
- To explore the potential of targeting MYH9 for controlling PRRSV infection.
Main Methods:
- Assessed the ability of human, mouse, and swine MYH9 to enhance PRRSV infection in pCD163-mediated cell lines.
- Utilized small interfering RNA (siRNA) and blebbistatin to inhibit MYH9 activity and evaluated the impact on PRRSV infection.
- Investigated the binding domain of MYH9 for PRRSV using recombinant MYH9 C-terminal fragments (PRA) and generated specific polyclonal antibodies against the MYH9 1676-1791 domain.
Main Results:
- MYH9 from different mammalian species (human, mouse, swine) accelerated PRRSV infection.
- Knockdown of MYH9 activity via siRNA or blebbistatin treatment significantly decreased PRRSV infection rates.
- A conserved binding domain (aa1676-1791) in the C-terminal fragment of MYH9 was identified for PRRSV binding.
- Recombinant MYH9 1676-1791 protein and specific polyclonal antibodies against this domain effectively inhibited PRRSV infection.
Conclusions:
- MYH9 acts as a critical cofactor, facilitating PRRSV entry into target cells.
- Targeting the MYH9 protein, particularly its conserved binding domain, presents a promising strategy for developing novel therapeutic agents against PRRSV infection.
