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Tytuł pozycji:

The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET

Tytuł :
The Structure of the Membrane Protein of SARS-CoV-2 Resembles the Sugar Transporter SemiSWEET
Autorzy :
Sunil Thomas
Pokaż więcej
Temat :
sars-cov-2, covid-19, coronavirus, virus, sugar transporter, semisweet, membrane glycoprotein, pandemic
Pathology
RB1-214
Immunologic diseases. Allergy
RC581-607
Źródło :
Pathogens and Immunity, Vol 5, Iss 1, Pp 342-363 (2020)
Wydawca :
Case Western Reserve University, 2020.
Rok publikacji :
2020
Kolekcja :
LCC:Pathology
LCC:Immunologic diseases. Allergy
Typ dokumentu :
article
Opis pliku :
electronic resource
Język :
English
ISSN :
2469-2964
Relacje :
https://paijournal.com/index.php/paijournal/article/view/377; https://doaj.org/toc/2469-2964
DOI :
10.20411/pai.v5i1.377
Dostęp URL :
https://doaj.org/article/5ea074f3a4b44216800bf3c74ca6a59c
Prawa :
Journal Licence: CC BY
Numer akcesji :
edsdoj.5ea074f3a4b44216800bf3c74ca6a59c
Czasopismo naukowe
Background: 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 has been 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). Methods: 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. Results: The M protein of SARS-CoV-2 is 98.6% similar to the M protein of bat SARS-CoV, maintains 98.2% homology with pangolin SARS-CoV, and has 90% homology with the M protein of SARS-CoV; whereas, the similarity is only 38% with the M protein of MERS-CoV. In silico analyses showed that the M protein of SARS-CoV-2 has a triple helix bundle, forms a single 3-transmembrane domain, and is homologous to the prokaryotic sugar transport protein SemiSWEET. SemiSWEETs are related to the PQ-loop family whose members function as cargo receptors in vesicle transport, mediate movement of basic amino acids across lysosomal membranes, and are also involved in phospholipase flippase function. Conclusions: The advantage and role of the M protein having a sugar transporter-like structure is not clearly understood. The M protein of SARS-CoV-2 interacts with S, E, and N protein. The S protein of the virus is glycosylated. It could be hypothesized that the sugar transporter-like structure of the M protein influences glycosylation of the S protein. 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. Overall, it could be hypothesized that the SemiSWEET sugar transporter-like structure of the M protein may be involved in multiple functions that may aid in the rapid proliferation, replication, and immune evasion of the SARS-CoV-2 virus. Biological experiments would validate the presence and function of the SemiSWEET sugar transporter.

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