LI Mingyang,SAIDU Kamara,WANG Qi, et al. The structure and immunodominant epitopes of SARS-CoV-2 E protein: an informatics prediction[J]. JOURNAL OF WEZHOU MEDICAL UNIVERSITY, 2021, 51(3): 209-214,219.
Abstract：Objective: To predict and analyze the structure and immunodominant epitope of envelope (E) protein of SARS-CoV-2 by bioinformatics. Methods: The amino acid sequence of SARS-CoV-2 E protein was retrieved from NCBI GenBank database, and its physicochemical properties, secondary structure and transmembrane
region were predicted by software on EXPASY server. A comprehensive analysis of transmembrane domain, hydrophilicity profile, surface probability, polarity, antigenicity index and flexibility was further made to predictB-cell epitopes of E protein; NetCTL 1.2 server was used to predict the T-cell antigen epitopes; the homology of E protein of coronavirus was analyzed by Vector NTI; the 3-dimension structural homology and functional domain of the E protein was modeled by Swiss Model. Results: SARS-CoV-2 E protein was a transmembrane protein composed of 75 amino acid residues, and the transmembrane region was mainlyαhelix. The protein may contain two B-cell epitopes and six CTL epitopes and its immunodominant epitope were probably in the regions of 16-34, 50-70 amino acids. SARS-CoV-2 E protein had high homology with SARS-CoV and Bat-SARS-like-CoV.The hydrophobic transmembrane domain and PDZ-binding motif were located in the N-terminal 12-34aa and Cterminal 72-75aa, respectively. Conclusion: E protein is a transmembrane domain protein, and the 16-34 and 50-70 amino acid regions of E protein are immunodominant epitopes, which provides a theoretical basis for the research on biological characteristics of SARS-CoV-2 E protein and vaccine.
