Molecules (Dec 2020)
Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features
- Sk. Sarif Hassan,
- Shinjini Ghosh,
- Diksha Attrish,
- Pabitra Pal Choudhury,
- Alaa A. A. Aljabali,
- Bruce D. Uhal,
- Kenneth Lundstrom,
- Nima Rezaei,
- Vladimir N. Uversky,
- Murat Seyran,
- Damiano Pizzol,
- Parise Adadi,
- Antonio Soares,
- Tarek Mohamed Abd El-Aziz,
- Ramesh Kandimalla,
- Murtaza M. Tambuwala,
- Gajendra Kumar Azad,
- Samendra P. Sherchan,
- Wagner Baetas-da-Cruz,
- Kazuo Takayama,
- Ángel Serrano-Aroca,
- Gaurav Chauhan,
- Giorgio Palu,
- Adam M. Brufsky
Affiliations
- Sk. Sarif Hassan
- Department of Mathematics, Pingla Thana Mahavidyalaya, Maligram 721140, India
- Shinjini Ghosh
- Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata 700009, India
- Diksha Attrish
- Dr. B. R. Ambedkar Centre for Biomedical Research (ACBR), University of Delhi (North Campus), Delhi 110007, India
- Pabitra Pal Choudhury
- Applied Statistics Unit, Indian Statistical Institute, Kolkata 700108, West Bengal, India
- Alaa A. A. Aljabali
- Department of Pharmaceutics and Pharmaceutical Technology, Yarmouk University-Faculty of Pharmacy, Irbid 566, Jordan
- Bruce D. Uhal
- Department of Physiology, Michigan State University, East Lansing, MI 48824, USA
- Kenneth Lundstrom
- PanTherapeutics, Rte de Lavaux 49, CH1095 Lutry, Switzerland
- Nima Rezaei
- Research Center for Immunodeficiencies, Pediatrics Center of Excellence, Children’s Medical Center, Tehran University of Medical Sciences, Tehran 1416753955, Iran
- Vladimir N. Uversky
- Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA
- Murat Seyran
- Doctoral studies in natural and technical sciences (SPL 44), University of Vienna, 1010 Wien, Austria
- Damiano Pizzol
- Italian Agency for Development Cooperation—Khartoum, Sudan Street 33, Al Amarat, Khartoum 825109, Sudan
- Parise Adadi
- Department of Food Science, University of Otago, Dunedin 9054, New Zealand
- Antonio Soares
- Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 77030, USA
- Tarek Mohamed Abd El-Aziz
- Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 77030, USA
- Ramesh Kandimalla
- Applied Biology, CSIR-Indian Institute of Chemical Technology Uppal Road, Tarnaka, Hyderabad 500007, India
- Murtaza M. Tambuwala
- School of Pharmacy and Pharmaceutical Science, Ulster University, Coleraine BT52 1SA, Northern Ireland, UK
- Gajendra Kumar Azad
- Department of Zoology, Patna University, Patna, Bihar 800005, India
- Samendra P. Sherchan
- Department of Environmental Health Sciences, Tulane University, New Orleans, LA 70112, USA
- Wagner Baetas-da-Cruz
- Translational Laboratory in Molecular Physiology, Centre for Experimental Surgery, College of Medicine, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro 21941901, Brazil
- Kazuo Takayama
- Center for iPS Cell Research and Application, Kyoto University, Kyoto 606-8501, Japan
- Ángel Serrano-Aroca
- Biomaterials and Bioengineering Lab, Translational Research Centre San Alberto Magno, Catholic University of Valencia San Vicente Mártir, c/Guillem de Castro 94, 46001 Valencia, Spain
- Gaurav Chauhan
- School of Engineering and Sciences, Tecnologico de Monterrey, Av. Eugenio Garza Sada 2501 Sur, Monterrey 64849, Nuevo León, Mexico
- Giorgio Palu
- Department of Molecular Medicine, University of Padova, Via Gabelli 63, 35121 Padova, Italy
- Adam M. Brufsky
- Division of Hematology/Oncology, Department of Medicine, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA
- DOI
- https://doi.org/10.3390/molecules25245906
- Journal volume & issue
-
Vol. 25,
no. 24
p. 5906
Abstract
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) that is engendering the severe coronavirus disease 2019 (COVID-19) pandemic. The spike (S) protein receptor-binding domain (RBD) of SARS-CoV-2 binds to the three sub-domains viz. amino acids (aa) 22–42, aa 79–84, and aa 330–393 of ACE2 on human cells to initiate entry. It was reported earlier that the receptor utilization capacity of ACE2 proteins from different species, such as cats, chimpanzees, dogs, and cattle, are different. A comprehensive analysis of ACE2 receptors of nineteen species was carried out in this study, and the findings propose a possible SARS-CoV-2 transmission flow across these nineteen species.
Keywords
