Abstract

PEDRO HUAMAN, Juan J.  and  MOYA CHAVEZ, Loana. In silico, structural and functional analysis of ace2 protein in different vertebrates and its relationship to SARS-COV-2. Arnaldoa [online]. 2024, vol.31, n.1, pp.151-169.  Epub Apr 20, 2024. ISSN 1815-8242.  http://dx.doi.org/10.22497/arnaldoa.311.31108.

At the end of 2019, a new infectious respiratory condition located in Hubei Wuhan-China province caused by SARS-CoV-2 virus was manifested. Moreover, angiotensin-converting enzyme 2 (ACE2) was quickly identified as the critical functional receptor for SARS-CoV-2. The study of the ACE2 protein allows us to determine the possible reservoirs that coronaviruses such as SARS-CoV, SARS-CoV-2 and others could have in nature. The present research aims to analyze structurally and functionally the ACE2 protein in different classes of vertebrates. For this purpose, a total of 35 amino acid sequences were recovered and a preliminary analysis was performed with ProtParam, SMART, InterPro and CATHdb. The secondary structure of the proteins of 10 selected species was predicted using the PSIPRED tool. Subsequently, tertiary structure was modeled with MODELLER 10.4 and validation was performed using Procheck. Refinement was performed using ModRefiner and GalaxyRefine tools, for structural alignment CLICK was used. It was observed that the physicochemical properties, domains and functions of the different vertebrate classes are very similar. Similarly, it can be observed that the secondary structure found with the highest prevalence in the proteins was the alpha helix. Finally, there is a high conservation in the three-dimensional structure when compared with that of Homo sapiens. This evolutionary conservation denotes its importance for living beings and indicates the potential susceptibility of different species to coronaviruses through the same ACE2 receptor.

Keywords : coronavirus; receptor; homology modeling; domains; alpha helix; hosts.

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