Abstract
The pandemic COVID-19 was caused by a novel Coronavirus-2 (SARS-CoV-2) that infects humans through the binding of glycosylated SARS-CoV-2 spike 2 protein to the glycosylated ACE2 receptor. The spike 2 protein recognizes the N-terminal helices of the glycosylated metalloprotease domain in the human ACE2 receptor. To understand the susceptibility of animals for infection and transmission, we did sequence and structure-based molecular interaction analysis of 16 ACE2 receptors from different mammalian species with SARS-CoV-2 spike 2 receptor binding domain. Our comprehensive structure analysis revealed that the natural substitution of amino acid residues Gln24, His34, Phe40, Leu79 and Met82 in the N-terminal α1 and α2 helices of the ACE2 receptor results in loss of crucial network of hydrogen-bonded and hydrophobic interactions with receptor binding domain of SARS-CoV-2 spike protein. Another striking observation is the absence of N-glycosylation site Asn103 in all mammals and many species, lack more than one N-linked glycosylation site in the ACE2 receptor. Based on the loss of crucial interactions and the absence of N-linked glycosylation sites we categorized Felis catus, Equus caballus, Panthera tigris altaica, as highly susceptible while Oryctolagus cuniculus, Bos Tauras, Ovis aries and Capra hircus as moderately susceptible species for infection. Similarly, the E. asinus, Bubalus bubalis, Canis lupus familiaris, Ailuropoda melaleuca and Camelus dromedarius are categorized as low susceptible with Loxodonta Africana, Mus musculus, Sus scrofa and Rattus rattus as least susceptible species for SARS-CoV-2 infection.Supplementary InformationThe online version contains supplementary material available at 10.1007/s13205-020-02599-2.
Highlights
COVID-19 is one of the most dreadful pandemic diseases of the 21st century responsible for most deaths worldwide
The absence of a glycosylation site at position Asn103 in all other mammals plays an essential role in spike recognition of the ACE2 receptor
Our study shows that natural substitution at crucial interacting regions and the loss of N-linked glycosylation sites in the ACE2 receptors makes animals less susceptible to infection, with no primary role in transmission
Summary
COVID-19 is one of the most dreadful pandemic diseases of the 21st century responsible for most deaths worldwide. The first human COVID-19 case was reported from Wuhan city, Hubei state of China, in December 2019 and expanded globally as a new health pandemic (Zhao et al 2020b) (Li et al 2020). As reported by World Health Organization till 12th December 2020, 69.5 million cases are confirmed with infection globally, and the total death is 1.5 million (World Health Organization). Hypothesized to have originated in bats with unknown intermediate hosts, this could be the result of a “spillover event”(WHO) (Banerjee et al 2019). Earlier studies described bats and pangolins as intermediate hosts (Zhang et al 2020a); subsequent literature failed to reveal any such connections (Zhang et al 2020b). Some of these coronaviruses can transmit between animals and humans
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