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Elastase-mediated membrane fusion of highly pathogenic porcine reproductive and respiratory syndrome virus at host cell surface

文献类型： 外文期刊

作者： Hou, Jie 1 ; Li, Rui 2 ; Qiao, Songlin 2 ; Chen, Xin-xin 2 ; Xing, Guangxu 2 ; Zhang, Gaiping 1 ;

作者机构： 1.Jilin Univ, Coll Vet Med, Changchun 130062, Peoples R China

2.Henan Acad Agr Sci, Key Lab Anim Immunol, Henan Prov Key Lab Anim Immunol, Minist Agr, 116 Huayuan Rd, Zhengzhou 450002, Henan, Peoples R China

3.Henan Agr Univ, Coll Anim Sci & Vet Med, 63 Nongye Rd, Zhengzhou 450002, Henan, Peoples R China

关键词： HP-PRRSV; Infection; Elastase; Membrane fusion; GP5

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.293； 五年影响因子：3.599 ）

ISSN： 0378-1135

年卷期： 2020 年 250 卷

页码：

收录情况： SCI

摘要： Infection by enveloped viruses includes endocytosis and/or membrane fusion at the plasma membrane, where host cell proteases play an essential role. Among them, elastase-mediated infection has been documented for several enveloped viruses. Porcine reproductive and respiratory syndrome virus (PRRSV), an economically critical factor in global swine industry, is previously reported to infect host cells via low pH-dependent clathrin-mediated endocytosis (CME) and undergo membrane fusion in recycling endosomes. In the current study, we identified that elastase was significantly elevated in the lung tissues of highly pathogenic PRRSV (HP-PRRSV)-infected pigs compared to the mock-infected ones. We subsequently demonstrated that elastase contributed to HP-PRRSV infection in both MARC-145 cells and porcine alveolar macrophages (PAMs). Mechanistically, HP-PRRSV entered host cells at the cell surface via elastase-mediated membrane fusion, independent of low pH and CME, and its glycoprotein 5 (GP5) was cleaved by the protease during this process. All these findings deepen our understanding of HP-PRRSV infection, and are beneficial for prevention and control of the disease.

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