SARS CoV-2 SPIKE GLYCOPROTEIN MUTATIONS AND CHANGES IN PROTEIN STRUCTURE

Severe Acute Respiratory Syndrome Corona Virus-2 (SARS CoV-2) is a single-stranded positive polarity RNA virus with high virulence effect. Spike (S) glycoprotein the outermost component of SARS CoV-2 virion and important in entry into cell via angiotensin converting enzyme 2 (ACE2) receptor. ACE2 plays an role regulation human blood pressure by vasoconstrictor to vasodilator 1-7. In this study, changes that mutations Asian isolates may cause S structure were analyzed modeled contribute drug vaccine targeting studies. Genome, proteome mutation analyses done using bioinformatics tools (MAFFT, MegaX, PSIPRED, MolProbity, PyMoL). Protein modelling was performed ProMod3. We detected 26 glycoprotein. The these reveal general topological conformational affect features CoV-2. It determined converted receptor binding domain (RBD) from down-formation like-up formation. thought change occurring after RBD increase affinity. These findings could be beneficial for disease prevention drug/vaccine development