Tags

Type your tag names separated by a space and hit enter

Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features.
Molecules. 2020 Dec 13; 25(24)M

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.

Authors+Show Affiliations

Department of Mathematics, Pingla Thana Mahavidyalaya, Maligram 721140, India.Department of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata 700009, India.Dr. B. R. Ambedkar Centre for Biomedical Research (ACBR), University of Delhi (North Campus), Delhi 110007, India.Applied Statistics Unit, Indian Statistical Institute, Kolkata 700108, West Bengal, India.Department of Pharmaceutics and Pharmaceutical Technology, Yarmouk University-Faculty of Pharmacy, Irbid 566, Jordan.Department of Physiology, Michigan State University, East Lansing, MI 48824, USA.PanTherapeutics, Rte de Lavaux 49, CH1095 Lutry, Switzerland.Research Center for Immunodeficiencies, Pediatrics Center of Excellence, Children's Medical Center, Tehran University of Medical Sciences, Tehran 1416753955, Iran. Network of Immunity in Infection, Malignancy and Autoimmunity (NIIMA), Universal Scientific Education and Research Network (USERN), SE-123 Stockholm, Sweden.Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.Doctoral studies in natural and technical sciences (SPL 44), University of Vienna, 1010 Wien, Austria.Italian Agency for Development Cooperation-Khartoum, Sudan Street 33, Al Amarat, Khartoum 825109, Sudan.Department of Food Science, University of Otago, Dunedin 9054, New Zealand.Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 77030, USA.Department of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr, San Antonio, TX 77030, USA. Zoology Department, Faculty of Science, Minia University, El-Minia 61519, Egypt.Applied Biology, CSIR-Indian Institute of Chemical Technology Uppal Road, Tarnaka, Hyderabad 500007, India. Department of Biochemistry, Kakatiya Medical College, Warangal, Telangana 500022, India.School of Pharmacy and Pharmaceutical Science, Ulster University, Coleraine BT52 1SA, Northern Ireland, UK.Department of Zoology, Patna University, Patna, Bihar 800005, India.Department of Environmental Health Sciences, Tulane University, New Orleans, LA 70112, USA.Translational Laboratory in Molecular Physiology, Centre for Experimental Surgery, College of Medicine, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro 21941901, Brazil.Center for iPS Cell Research and Application, Kyoto University, Kyoto 606-8501, Japan.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.School of Engineering and Sciences, Tecnologico de Monterrey, Av. Eugenio Garza Sada 2501 Sur, Monterrey 64849, Nuevo León, Mexico.Department of Molecular Medicine, University of Padova, Via Gabelli 63, 35121 Padova, Italy.Division of Hematology/Oncology, Department of Medicine, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

33322198

Citation

Hassan, Sk Sarif, et al. "Possible Transmission Flow of SARS-CoV-2 Based On ACE2 Features." Molecules (Basel, Switzerland), vol. 25, no. 24, 2020.
Hassan SS, Ghosh S, Attrish D, et al. Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features. Molecules. 2020;25(24).
Hassan, S. S., Ghosh, S., Attrish, D., Choudhury, P. P., Aljabali, A. A. A., Uhal, B. D., Lundstrom, K., Rezaei, N., Uversky, V. N., Seyran, M., Pizzol, D., Adadi, P., Soares, A., El-Aziz, T. M. A., Kandimalla, R., Tambuwala, M. M., Azad, G. K., Sherchan, S. P., Baetas-da-Cruz, W., ... Brufsky, A. M. (2020). Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features. Molecules (Basel, Switzerland), 25(24). https://doi.org/10.3390/molecules25245906
Hassan SS, et al. Possible Transmission Flow of SARS-CoV-2 Based On ACE2 Features. Molecules. 2020 Dec 13;25(24) PubMed PMID: 33322198.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features. AU - Hassan,Sk Sarif, AU - Ghosh,Shinjini, AU - Attrish,Diksha, AU - Choudhury,Pabitra Pal, AU - Aljabali,Alaa A A, AU - Uhal,Bruce D, AU - Lundstrom,Kenneth, AU - Rezaei,Nima, AU - Uversky,Vladimir N, AU - Seyran,Murat, AU - Pizzol,Damiano, AU - Adadi,Parise, AU - Soares,Antonio, AU - El-Aziz,Tarek Mohamed Abd, AU - Kandimalla,Ramesh, AU - Tambuwala,Murtaza M, AU - Azad,Gajendra Kumar, AU - Sherchan,Samendra P, AU - Baetas-da-Cruz,Wagner, AU - Takayama,Kazuo, AU - Serrano-Aroca,Ángel, AU - Chauhan,Gaurav, AU - Palu,Giorgio, AU - Brufsky,Adam M, Y1 - 2020/12/13/ PY - 2020/11/04/received PY - 2020/12/10/revised PY - 2020/12/10/accepted PY - 2020/12/16/entrez PY - 2020/12/17/pubmed PY - 2020/12/23/medline KW - ACE2 KW - SARS-CoV-2 KW - bioinformatics KW - transmission KW - viral spike receptor-binding domain JF - Molecules (Basel, Switzerland) JO - Molecules VL - 25 IS - 24 N2 - 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. SN - 1420-3049 UR - https://www.unboundmedicine.com/medline/citation/33322198/Possible_Transmission_Flow_of_SARS_CoV_2_Based_on_ACE2_Features_ L2 - https://www.mdpi.com/resolver?pii=molecules25245906 DB - PRIME DP - Unbound Medicine ER -