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Abstract

IN SILICO STUDY AND VALIDATION OF SARS CORONAVIRUS-2 (COVID19) PROTEINS FOR BETTER UNDERSTANDING THE CONTROL MEASURES

Ashokan Kannarath*, Koshti V. Vijay, Mundaganur D. S. and Mundaganur Y. D.

ABSTRACT

SARS Corona Virus-2 (COVID19) protein sequences of nucleocapsid Phosphoprotein (N), membrane glycoprotein (M), envelope protein (E) and surface (spike) glycoprotein (S) was evaluated with bioinformatics servers and tools. The study revealed that membrane protein shows highest percentage of amino acid (>100) and the least (97.9) in Sprotein. The bit score also shows the same trend but envelope protein shows the least bit score and maximum E-value, a positive correlation. The amino acid composition shows that all the proteins studied are rich in Leucine except N- protein which contains more glycine. Pyrrolysine, selenocystein and cysteine are absent in all the proteins studied, an indication of low thermo stability. The physico-chemical studies shows that except spike protein all other proteins studied are positively charged due to aspartic acid and glutamic acid, but S-protein is negatively charged. EC is maximum in S protein and minimum in E protein. Instability index (II) shows that N and S proteins are more stable. Further all proteins are hydrophobic except E- protein. We also generate 3D model and the model was evaluated and observed that the 3D structure falls in the accepted limits. The study also focused on phosphorylation site, transmembrane sequence and hydrophobic residues. The N-glycosylation site prediction showed that it is very poor in N, E protein and totally absent in M-protein and more in S-protein. The practical implication of the study is that the result will assists the scientist and technicians related to control the SARS Corona Virus -2 (COVID19) in better way.

Keywords: SARS Coronavirus-2, Physico-chemical parameters, phosphorylation site, N-Glycosylation, hydrophobic residues and transmembrane protein.


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