Department of Comparative Physiology, Uppsala University, Uppsala, Sweden.
Department of Comparative Physiology, Uppsala University, Uppsala, Sweden.
Fish Shellfish Immunol. 2017 Sep;68:211-219. doi: 10.1016/j.fsi.2017.07.026. Epub 2017 Jul 10.
Serine proteases are involved in many critical physiological processes including virus spread and replication. In the present study, we identified a new clip-domain serine protease (PlcSP) in the crayfish Pacifastacus leniusculus hemocytes, which can interact with the White Spot Syndrome Virus (WSSV) envelope protein VP28. It was characterized by a classic clip domain with six strictly conserved Cys residues, and contained the conserved His-Asp-Ser (H-D-S) motif in the catalytic domain. Furthermore, signal peptide prediction revealed that it has a 16-residue secretion signal peptide. Tissue distribution showed that it was mainly located in P. leniusculus hemocytes, and its expression was increased in hemocytes upon WSSV challenge. In vitro knock down of PlcSP decreased both the expression of VP28 and the WSSV copy number in hematopoietic stem (HPT) cells. Accordingly, these data suggest that the new serine protease may be of importance for WSSV infection into hematopoietic cells.
丝氨酸蛋白酶参与许多关键的生理过程,包括病毒的传播和复制。在本研究中,我们在螯虾血细胞中鉴定了一种新的 clip 结构域丝氨酸蛋白酶(PlcSP),它可以与白斑综合征病毒(WSSV)包膜蛋白 VP28 相互作用。它具有典型的 clip 结构域,包含六个严格保守的半胱氨酸残基,并在催化结构域中含有保守的 His-Asp-Ser(H-D-S)基序。此外,信号肽预测表明它具有 16 个残基的分泌信号肽。组织分布表明它主要位于螯虾血细胞中,并且在 WSSV 攻击时其在血细胞中的表达增加。体外敲低 PlcSP 降低了造血干细胞(HPT)细胞中 VP28 的表达和 WSSV 拷贝数。因此,这些数据表明该新的丝氨酸蛋白酶可能对 WSSV 感染造血细胞具有重要意义。