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Comparative Genomics of Receptor Binding Domains of Spike Protein and Receptor Interaction in COVID-19 Patient




The current outbreak of viral pneumonia in the city of Wuhan, China, was caused by a novel coronavirus designated 2019-nCoV, as determined by sequencing the viral RNA genome. Among its genome, S protein is surface-exposed and mediates entry into host cells. Currently it is one of the main targets for designing antibodies (Abs), therapeutic and vaccine. Earlier studies stated that ACE2 (angiotensin converting enzyme 2) could facilitate S protein mediated entry for this newly emerged coronavirus. Here we have taken an attempt to compare the genetic structure of receptor binding domain within S protein of highly pathogenic human coronaviruses (special reference to 2019-nCoV) with Bat coronavirus RaTG13. We have compared 2019-nCov receptor binding domain (RBD) with other pathogenic human coronaviruses (MERS-CoV and SARS-CoV) and Bat coronavirus RaTG13. We found that it is closest to RaTG13 RBD than MERS-CoV and SARS-CoV. Our study shows that 2019-nCov RBD also has significant identity with pangolin S protein RBD. We have also predicted the amino acid residues within RDB those may play important role for ACE2 receptor interaction. We identified unique signature for furin cleavage in 2019-nCov S protein but not in of other pathogenic human coronaviruses (tested here), bat coronavirus RaTG13 or pangolin.


Coronavirus, sequence alignment, receptor binding domain


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