Structural comparison of CD163 SRCR5 from different species sheds some light on its involvement in porcine reproductive and respiratory syndrome virus-2 infection in vitro
文献类型: 外文期刊
作者: Ma, Hongfang 1 ; Li, Rui 2 ; Jiang, Longguang 3 ; Qiao, Songlin 2 ; Chen, Xin-Xin 2 ; Wang, Aiping 1 ; Zhang, Gaiping 1 ;
作者机构: 1.Zhengzhou Univ, Sch Life Sci, Zhengzhou 450001, Henan, Peoples R China
2.Henan Acad Agr Sci, Key Lab Anim Immunol, Henan Prov Key Lab Anim Immunol, Minist Agr, Zhengzhou 450002, Henan, Peoples R China
3.Fuzhou Univ, Coll Chem, Fuzhou 350116, Fujian, Peoples R China
4.Henan Agr Univ, Coll Vet Med, Zhengzhou 450002, Henan, Peoples R China
5.Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Jiangsu, Peoples R China
关键词: PRRSV; CD163; SRCR5; Crystal structure; Infection
期刊名称:VETERINARY RESEARCH ( 影响因子:3.699; 五年影响因子:4.113 )
ISSN: 0928-4249
年卷期: 2021 年 52 卷 1 期
页码:
收录情况: SCI
摘要: Porcine reproductive and respiratory syndrome (PRRS) is a serious disease burdening global swine industry. Infection by its etiological agent, PRRS virus (PRRSV), shows a highly restricted tropism of host cells and has been demonstrated to be mediated by an essential scavenger receptor (SR) CD163. CD163 fifth SR cysteine-rich domain (SRCR5) is further proven to play a crucial role during viral infection. Despite intense research, the involvement of CD163 SRCR5 in PRRSV infection remains to be elucidated. In the current study, we prepared recombinant monkey CD163 (moCD163) SRCR5 and human CD163-like homolog (hCD163L1) SRCR8, and determined their crystal structures. After comparison with the previously reported crystal structure of porcine CD163 (pCD163) SRCR5, these structures showed almost identical structural folds but significantly different surface electrostatic potentials. Based on these differences, we carried out mutational research to identify that the charged residue at position 534 in association with the one at position 561 were important for PRRSV-2 infection in vitro. Altogether the current work sheds some light on CD163-mediated PRRSV-2 infection and deepens our understanding of the viral pathogenesis, which will provide clues for prevention and control of PRRS.
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