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Notable sequence homology of the ORF10 protein introspects the architecture of SARS-CoV-2.

Authors :
Hassan SS
Attrish D
Ghosh S
Choudhury PP
Uversky VN
Aljabali AAA
Lundstrom K
Uhal BD
Rezaei N
Seyran M
Pizzol D
Adadi P
Soares A
Abd El-Aziz TM
Kandimalla R
Tambuwala MM
Azad GK
Sherchan SP
Baetas-da-Cruz W
Lal A
Palù G
Takayama K
Serrano-Aroca Á
Barh D
Brufsky AM
Source :
International journal of biological macromolecules [Int J Biol Macromol] 2021 Jun 30; Vol. 181, pp. 801-809. Date of Electronic Publication: 2021 Apr 16.
Publication Year :
2021

Abstract

The current Coronavirus Disease 19 (COVID-19) pandemic, caused by Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) shows similar pathology to MERS and SARS-CoV, with a current estimated fatality rate of 1.4%. Open reading frame 10 (ORF10) is a unique SARS-CoV-2 accessory protein, which contains eleven cytotoxic T lymphocyte (CTL) epitopes each of nine amino acids in length. Twenty-two unique SARS-CoV-2 ORF10 variants have been identified based on missense mutations found in sequence databases. Some of these mutations are predicted to decrease the stability of ORF10 in silico physicochemical and structural comparative analyses were carried out on SARS-CoV-2 and Pangolin-CoV ORF10 proteins, which share 97.37% amino acid (aa) homology. Though there is a high degree of ORF10 protein similarity of SARS-CoV-2 and Pangolin-CoV, there are differences of these two ORF10 proteins related to their sub-structure (loop/coil region), solubility, antigenicity and shift from strand to coil at aa position 26 (tyrosine). SARS-CoV-2 ORF10, which is apparently expressed in vivo since reactive T cell clones are found in convalescent patients should be monitored for changes which could correlate with the pathogenesis of COVID-19.<br />Competing Interests: Declaration of competing interest The authors do not have any conflicts of interest to declare.<br /> (Copyright © 2021 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1879-0003
Volume :
181
Database :
MEDLINE
Journal :
International journal of biological macromolecules
Publication Type :
Academic Journal
Accession number :
33862077
Full Text :
https://doi.org/10.1016/j.ijbiomac.2021.03.199