“…Additionally, upon observing the binding modes of ACE2-SARS-CoV-2 S-protein in human and snake, three regions of snake ACE2 with large structural differences were observed. Within these regions, one compact yet complicated polar interaction network was formed between hACE2 and the S-protein of SARS-CoV-2, yet these polar contacts were not present in snake ACE2, which is the main reason for the reduced ability of snake ACE2 to bind SARS-CoV-2 [98][99][100][101][102]. Further to this, Luan et al [91] have generated structural simulations showing several key contacts of hACE2 with SARS-CoV-2 RBD and found that in snake ACE2, these contacts were completely eradicated.…”
The emergence of multiple variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) highlights the importance of possible animal-to-human (zoonotic) and human-to-animal (zooanthroponotic) transmission and potential spread within animal species. A range of animal species have been verified for SARS-CoV-2 susceptibility, either in vitro or in vivo. However, the molecular bases of such a broad host spectrum for the SARS-CoV-2 remains elusive. Here, we structurally and genetically analysed the interaction between the spike protein, with a particular focus on receptor binding domains (RBDs), of SARS-CoV-2 and its receptor angiotensin-converting enzyme 2 (ACE2) for all conceivably susceptible groups of animals to gauge the structural bases of the SARS-CoV-2 host spectrum. We describe our findings in the context of existing animal infection-based models to provide a foundation on the possible virus persistence in animals and their implications in the future eradication of COVID-19.
“…Additionally, upon observing the binding modes of ACE2-SARS-CoV-2 S-protein in human and snake, three regions of snake ACE2 with large structural differences were observed. Within these regions, one compact yet complicated polar interaction network was formed between hACE2 and the S-protein of SARS-CoV-2, yet these polar contacts were not present in snake ACE2, which is the main reason for the reduced ability of snake ACE2 to bind SARS-CoV-2 [98][99][100][101][102]. Further to this, Luan et al [91] have generated structural simulations showing several key contacts of hACE2 with SARS-CoV-2 RBD and found that in snake ACE2, these contacts were completely eradicated.…”
The emergence of multiple variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) highlights the importance of possible animal-to-human (zoonotic) and human-to-animal (zooanthroponotic) transmission and potential spread within animal species. A range of animal species have been verified for SARS-CoV-2 susceptibility, either in vitro or in vivo. However, the molecular bases of such a broad host spectrum for the SARS-CoV-2 remains elusive. Here, we structurally and genetically analysed the interaction between the spike protein, with a particular focus on receptor binding domains (RBDs), of SARS-CoV-2 and its receptor angiotensin-converting enzyme 2 (ACE2) for all conceivably susceptible groups of animals to gauge the structural bases of the SARS-CoV-2 host spectrum. We describe our findings in the context of existing animal infection-based models to provide a foundation on the possible virus persistence in animals and their implications in the future eradication of COVID-19.
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