Mutational insights into the envelope protein of SARS-CoV-2.

Autor: Rahman MS; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh., Hoque MN; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh.; Department of Gynecology, Obstetrics and Reproductive Health, Bangabandhu Sheikh Mujibur Rahman Agricultural University, Gazipur 1706, Bangladesh., Islam MR; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh., Islam I; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh., Mishu ID; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh., Rahaman MM; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh., Sultana M; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh., Hossain MA; Department of Microbiology, University of Dhaka, Dhaka 1000, Bangladesh.
Jazyk: angličtina
Zdroj: Gene reports [Gene Rep] 2021 Mar; Vol. 22, pp. 100997. Date of Electronic Publication: 2020 Dec 08.
DOI: 10.1016/j.genrep.2020.100997
Abstrakt: The ongoing mutations in the structural proteins of SARS-CoV-2 are the major impediment for prevention and control of the COVID-19 disease. Presently we focused on evolution of the envelope (E) protein, one of the most enigmatic and less studied protein among the four structural proteins (S, E, M and N) associated with multitude of immunopathological functions of SARS-CoV-2. In the present study, we comprehensively analyzed 81,818 high quality E protein sequences of SARS-CoV-2 globally available in the GISAID database as of 20 August 2020. Compared to Wuhan reference strain, our mutational analysis explored only 1.2 % (982/81818) mutant strains undergoing a total of 115 unique amino acid (aa) substitutions in the E protein, highlighting the fact that most (98.8 %) of the E protein of SARS-CoV-2 strains are highly conserved. Moreover, we found 58.77 % (134 of 228) nucleotides (nt) positions of SARS-CoV-2 E gene encountering a total of 176 unique nt-level mutations globally, which may affect the efficacy of real time RT-PCR-based molecular detection of COVID-19. Importantly, higher aa variations observed in the C-terminal domain (CTD) of the E protein, particularly at Ser 55 -Phe 56 , Arg 69 and the C-terminal end (DLLV: 72-75) may alter the binding of SARS-CoV-2 Envelope protein to tight junction-associated PALS1 and thus could play a key role in COVID-19 pathogenesis. Furthermore, this study revealed the V25A mutation in the transmembrane domain which is a key factor for the homopentameric conformation of E protein. Our analysis also observed a triple cysteine motif harboring mutation (L39M, A41S, A41V, C43F, C43R, C43S, C44Y, N45R) which may hinder the binding of E protein with spike glycoprotein. These results therefore suggest the continuous monitoring of the structural proteins including the envelope protein of SARS-CoV-2 since the number of genome sequences from across the world are continuously increasing.
Competing Interests: The authors declare no conflict of interests.
(© 2020 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: