Abstract：Abstract: In order to explore the effect of type Ⅱ transmembrane serine protease (TMPRSS2) recombinant protein on blocking severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, a pseudovirus infected cell system was constructed in vitro, and vesicular stomatitis virus (ΔG-VSV/luciferase) pseudovirus carrying SARS-CoV-2 spike glycoprotein (S protein) was used for evaluating cell infection efficiency. The re-combinant TMPRSS2-Fc protein with enzyme activity and self-shearing site mutation was purified from 293F cells in vitro. It was found that the purified TMPRSS2-Fc recombinant protein with two mutations of shearing site R255Q and enzyme activity site S441A could effectively reduce the binding of S protein to TMPRSS2 on the surface of host cells, and block the infection of Calu3 lung cancer cell line with pseu-dovirus. These results indicated that the recombinant TMPRSS2-Fc protein could compete with the host co-receptor TMPRSS2 to bind to the S protein, blocking the cleavage and activation of S protein and inhibiting the membrane fusion between the virus and host cells, therefore stopping virus invasion. Overall, this study provides a new clue for preventing SARS-CoV-2 infection.
引用本文:
潘 婷, 彭倩文, 杜艳芸, 王晨辉. TMPRSS2重组蛋白阻断SARS-CoV-2假病毒的感染[J]. 生命科学研究, 2022, 26(4): 283-290. PAN Ting, PENG Qian-wen, DU Yan-yun, WANG Chen-hui. Recombinant TMPRSS2-Fc Protein Blocks SARS-CoV-2 Pseudovirus Infection. Life Science Research, 2022, 26(4): 283-290.
