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Li Sicong described the stability of the HCOV-NL63 coronavirus spike protein variant site from four dimensions.
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Abstract: By comparing themultiple sequence alignment results of both complete genome sequence and receptor-binding Spike (S) protein of human coronavirus NL63, we discovered that within the genome sequence the similarity of S protein was low, thus meaning there were mutations existing within S protein region. By contrast, there were only three amino acid mutations in the amino acid sequence of S protein. Therefore, in this dissertation, we further characterized the S protein of HCoV-NL63 and located key residues of RBD-receptor association through the virus S protein phylogeny analysis, using Pymol to construct protein conformation on three mutant sites, analyzing its effects on HCOV-NL63 S protein and using ProSNEx to determine hot spot residues in the viral-receptor binding domain. Our results showed that: the S protein of HCoV-NL63 was highly-conserved and the mutations had occurred within the S protein played an important role in stabilizing the structure of S protein. As HCoV-NL63 showed that the more stable the S protein was, the more affinitive it becameto bind human receptor ACE2. Therefore, we believe that HCOV-NL63 will coexist with human for a long time and its invasion and infection ability will gradually increase. The Aa353 and Aa354 are the main binding residues on receptor ACE2and Aa494-499 and Aa535-540 within RBD were important for receptor binding and virus entry.
