The Effects of SARS CoV-2 nsp13 Mutations on the Structure and Stability of Helicase in Chinese Isolates

Objective: Coronavirus Disease 2019 (COVID19) is a viral disease caused by Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2). The high mutation propensity of the SARS CoV-2 genome one biggest threats to long-term validity treatment options. Helicases are anti-viral targets because vital role they play in life cycle. In this study, changes protein structure nsp13 mutations were investigated contribute development effective antiviral drugs. Materials and Methods: Genome data 298 individuals located China location examined. mutant model was built using deep learning algorithms. Model quality assessment done with QMEAN. Protein stability analyses performed DynaMut2 Cutoff Scanning Matrix stability. Changes substrate affinity Haddock v2.4. Results: twenty-eight identified (23 sense, 5 missense). five missense (Leu14Phe, Arg15Ser, Arg21Ser, Leu235Phe, Ala454Thr) modeled. decrease helicase (-0.99, -1.66, -1.15, -0.54, -0.73 for Leu14Phe, Ala454Thr, respectively). reduced helicase's substrate. docking scores wild-type -84.4±1.4 kcal.mol-1 -71.1±6.7 kcal.mol-1, respectively. Conclusion: Helicase nucleic acid helicase. results provide important on potential antivirals effect functions proteins.