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: Received: 28 April 2020 / Approved: 29 April 2020 / Online: 29 April 2020 (14:06:19 CEST)
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: Received: 3 May 2020 / Approved: 4 May 2020 / Online: 4 May 2020 (18:14:23 CEST)
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: Received: 19 May 2020 / Approved: 20 May 2020 / Online: 20 May 2020 (04:43:42 CEST)
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: Received: 18 July 2020 / Approved: 19 July 2020 / Online: 19 July 2020 (15:06:53 CEST)
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: Received: 19 August 2020 / Approved: 20 August 2020 / Online: 20 August 2020 (13:47:23 CEST)
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: Received: 17 October 2020 / Approved: 19 October 2020 / Online: 19 October 2020 (10:48:05 CEST)
Thomas, S. The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET. Pathogens and Immunity. 2020;5(1):342-363.
Thomas, S. The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET. Pathogens and Immunity. 2020;5(1):342-363.
Thomas, S. The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET. Pathogens and Immunity. 2020;5(1):342-363.
Thomas, S. The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET. Pathogens and Immunity. 2020;5(1):342-363.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the disease COVID-19 that has decimated the health and economy of our planet. The virus causes the disease not only in people but also in companion and wild animals. People with diabetes are at risk of the disease. As yet we do not know why the virus is highly successful in causing the pandemic within 3 months of its first report. The structural proteins of SARS include, membrane glycoprotein (M), envelope protein (E), nucleocapsid protein (N) and the spike protein (S). The structure and function of the most abundant structural protein of SARS-CoV-2, the membrane (M) glycoprotein is not fully understood. Using in silico analyses we determined the structure and potential function of the M protein. In silico analyses showed that the M protein of SARS-CoV-2 has a triple helix bundle, form a single 3-transmembrane domain (TM), and are homologous to the prokaryotic sugar transport protein semiSWEET. SemiSWEETs are related to the PQ-loop family that function as cargo receptors in vesicle transport, mediates movement of basic amino acids across lysosomal membranes, and is also involved in phospholipase flippase function. The advantage and role of sugar transporter-like structure in viruses is unknown. Endocytosis is critical for the internalization and maturation of RNA viruses, including SARS-CoV-2. Sucrose is involved in endosome and lysosome maturation and may also induce autophagy, pathways that help in the entry of the virus. It could be hypothesized that the semiSWEET sugar transporters could be used in multiple pathways that may aid in the rapid proliferation and replication of the virus. Biological experiments would validate the presence and function of the semiSWEET sugar transporter.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Commenter: Sunil Thomas
Commenter's Conflict of Interests: Author