Structural basis for the recognition of HCoV-HKU1 by human TMPRSS2  

作　　者：Lingyun Xia Yuanyuan Zhang Qiang Zhou 

机构地区：[1]Center for Infectious Disease Research,Research Center for Industries of the Future,Zhejiang Key Laboratory of Structural Biology,School of Life Sciences,Westlake University.Institute of Biology,Westlake Institute for Advanced Study,Hangzhou,Zhejiang,China. [2]Westlake Laboratory of Life Sciences and Biomedicine,Hangzhou,Zhejiang,China.

出　　处：《Cell Research》2024年第7期526-529,共4页细胞研究（英文版）

基　　金：the National Natural Science Foundation of China(82241081);the Key Regional Research and Development Program(2023CSJZN0600);Ministry of Science and Technology of China,and the Hangzhou agricultural and social development scientific research project(202204B14).

摘　　要：Dear Editor,Human coronaviruses are pathogens capable of causing respiratory illnesses in humans,with seven identified species,1 three of which have caused epidemics or global pandemics in the past two decades,namely,Severe Acute Respiratory Syndrome Coronavirus(SARS-CoV),2 Middle East Respiratory Syndrome Coronavirus(MERS-CoV),3 and Severe Acute Respiratory Syndrome Coronavirus 2(SARS-CoV-2).4 Along with these three viruses,HCoV-HKU1(HKU1)belongs to theβ-coronavirus genus.With three serotypes(HKU1-A,HKU1-B,and HKU1-C),HKU1 infection commonly causes the common cold,but also leads to severe lower respiratory tract infections.5 The spike(S)protein of HKU1 plays a crucial role in cell invasion by binding to host receptors,with the transmembrane serine protease TMPRSS2 recently identified as its protein receptor.6 TMPRSS2 comprises intracellular,transmembrane,LDL receptor A(LDLR-A,residues 112–149),scavenger receptor cysteine-rich(SRCR,residues 150–242),and C-terminal serine protease(SP,residues 256–489)domains.However,the structural basis of TMPRSS2 interaction with the S protein remains elusive.

关 键 词：TMPRSS2 ACUTE INVASION 

分 类 号：R373[医药卫生—病原生物学]