Bioinformatics analysis of TMPRSS2, a key protease used by SARS-CoV-2 to invade host cells

ABSTRACT

Through bioinformatics, we systematically predicted and analyzed the structure and function of TMPRSS2, a key protease used by SARS-CoV-2 to invade host cells, thus providing a reliable reference for the research on the protein and the development of its inhibitors. We used ProtParam, Protscale, SignalP 4.0 Server, SecretomeP 2.0 server, TMHMM Server v. 2.0, SOPMA, SWISS-MODEL, MEGA-X and other software to predict the structure, function, evolution, biological processes and other aspects of the TMPRSS2 gene and protein. We comprehensively analyzed and demonstrated the results obtained with each program. TMPRSS2 protein was found to be a hydrophilic protein composed of 492 amino acids. It has a transmembrane helix structure and is a non-classical secreted protein. The expression of TMPRSS2 protein in the prostate was particularly abundant, and it has abundant post-translational modification sites. TMPRSS2 protein has a total of three superfamily conserved domains, and the amino acid sequence after the 100th position is relatively conserved. We report comprehensive prediction and analysis of the structure and function of the TMPRSS2 protein. From the perspective of bioinformatics, our results verify its characteristics as a serine protease and provide a possible mechanistic explanation for its participation in SARS-CoV-2 invasion of hosts. This work should facilitate further experiments and research related to TMPRSS2.