ウイルス学と真菌学
オープンアクセス

概要

Corona Virus ORF1ab-Derived Nsp9 and Nsp10Non-Structural Proteins have Homologies to S8/S10 Ribosomal Proteins as well as RlmG/ ErmDrRNAMethyltransferasesand may Inhibit Host Mitoribosome Assembly and Protein Synthesis

Asit Kumar Chakraborty

Multi-Alignment method coupled with phylogenetic analysis we disclosed the Nsp9 and Nsp10 non-structural proteins of Corona Virus asrRNARlmH/K methyltransferases with similarities with bin recombinase and int-core integrase fold. Further, Nsp9 has similarities to S8 ribosomal protein and Nap10 has similarity to S10 ribosomal protein. Previously, we showed Nsp13, Nsp14, Nsp15 and Nsp16 are also different types of rRNARlmE/N and Cfr-like methyltransferases-ribonucleasewith RNA helicase domains. Two domains of Nsp13 astonishingly have similarities to ribosomal proteins L6 and L9. Taken together, Nsp9/10 and Nsp13-16 proteins could mimic host ribosome assembly and also could methylate rRNA of mitobibosome preventing mitochondrial protein synthesis and oxidative phosphorylation. Low ATP synthesis causes lowering blood pressure following coma but very ATP concentration (1-10nM) surely induces platelets aggregation through vWA, collagen and GpIIb/IIIaproteins followed byfibrin formation and blood clotting as recently have seen in the lung of many Corona virus infected patients. We have also postulated that two polyproteins itself resemble like 28S and 38S mitoribosome subunits and compete with rRNAs inhibiting the ribosome turnover and new protein synthesis due to their similarities with many ribosomal proteins.Such finding may be valuable in computer-based novel drug design against Corona virus.