Prediction and Evolution of B Cell Epitopes of Surface Protein in SARS-CoV-2

Jerome R Lon; Yunmeng Bai; Bingxu Zhong; Fuqiang Cai; Hongli Du

The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.04.03.022723 doi: bioRxiv preprint hydrophilicity. The score of hydrophilicity and hydrophobicity on the polypeptide chain of S protein constantly fluctuates, with most of the scores being negative, which revealed the possibility that the protein had bisexual properties on the basis of hydrophilicity. B. The E protein has a maximum score of hydrophobicity, 3.489 at the 21 st and the 25 th site, which revealed a strong hydrophobicity; a minimum score of hydrophobicity, -1.550 at the 65 th site, which revealed a strong hydrophilicity. Most of the scores of the residues being positive, which revealed the possibility that the protein has obvious hydrophobicity. C. The M protein has a maximum score of hydrophobicity, 2.978 at the 84 th site, which revealed a strong hydrophobicity; a minimum score of Table 2 The composition and the antigenic index of the epitopes of SARS-CoV-2