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http://krishi.icar.gov.in/jspui/handle/123456789/76675
Title: | A novel structure-based approach for identification of vertebrate susceptibility to SARS-CoV-2: Implications for future surveillance programmes |
Authors: | Kaushik, R. Kumar, N. Zhang, K. Y. J. Srivastava, P. Bhatia, S. Malik, Y. S. |
ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
Author's Affiliated institute: | Laboratory for Structural Bioinformatics, Center for Biosystems Dynamics Research, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa, 230-0045, Japan. Zoonotic Diseases Group, ICAR- National Institute of High Security Animal Diseases, Bhopal, 462022, India. College of Animal Biotechnology, Guru Angad Dev Veterinary and Animal Science University (GADVASU), Ludhiana, 141004, Punjab, India |
Published/ Complete Date: | 2022-04-20 |
Project Code: | Not Available |
Keywords: | ACE2; Binding affinity; Dissociation constant; Host range; SARS-CoV-2; Spike protein; Vertebrate species. |
Publisher: | Elsevier Inc. |
Citation: | Kaushik, R., Kumar, N., Zhang, K. Y. J., Srivastava, P., Bhatia, S., & Malik, Y. S. (2022). A novel structure-based approach for identification of vertebrate susceptibility to SARS-CoV-2: Implications for future surveillance programmes. Environmental research, 212(Pt C), 113303. |
Series/Report no.: | Not Available; |
Abstract/Description: | Understanding the origin of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been a highly debatable and unresolved issue for scientific communities all over the world. Understanding the mechanism of virus entry to the host cells is crucial to deciphering the susceptibility profiles of animal species to SARS-CoV-2. The interaction of SARS-CoV-2 ligands (receptor-binding domain on spike protein) with its host cell receptor, angiotensin-converting enzyme 2 (ACE2), is a critical determinant of host range and cross-species transmission. In this study, we developed and implemented a rigorous computational approach for predicting binding affinity between 299 ACE2 orthologs from diverse vertebrate species and the SARS-CoV-2 spike protein. The findings show that the SARS-CoV-2 spike protein can bind to a wide range of vertebrate species carrying evolutionary divergent ACE2, implying a broad host range at the virus entry level, which may contribute to cross-species transmission and further viral evolution. Furthermore, the current study facilitated the identification of genetic determinants that may differentiate susceptible from resistant host species based on the conservation of ACE2-spike protein interacting residues in vertebrate host species known to facilitate SARS-CoV-2 infection; however, these genetic determinants warrant in vivo experimental confirmation. The molecular interactions associated with varied binding affinity of distinct ACE2 isoforms in a specific bat species were identified using protein structure analysis, implying the existence of diversified bat species' susceptibility to SARS-CoV-2. The current study's findings highlight the importance of intensive surveillance programmes aimed at identifying susceptible hosts, especially those with the potential to transmit zoonotic pathogens, in order to prevent future outbreaks. |
Description: | Not Available |
ISSN: | 0013-9351 |
Type(s) of content: | Journal |
Sponsors: | Not Available |
Language: | English |
Name of Journal: | Environmental Research |
Journal Type: | Included NAAS journal |
NAAS Rating: | 14.43 |
Impact Factor: | 8.43 |
Volume No.: | 212(Pt C) |
Page Number: | 113303 |
Name of the Division/Regional Station: | Not Available |
Source, DOI or any other URL: | 10.1016/j.envres.2022.113303 |
URI: | http://krishi.icar.gov.in/jspui/handle/123456789/76675 |
Appears in Collections: | AS-NIHSAD-Publication |
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