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Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study
Ebtisam A Aldaais1, Subha Yegnaswamy2, Fatimah Albahrani3
1Department of Radiological Sciences, Imam Abdulrahman Bin Faisal University, Dammam, P.O. Box 2435, 31441, Saudi Arabia.
Abstract:
The outbreak of SARS in 2003, MERS in 2012, and now COVID-19 in 2019 has demonstrated that Coronaviruses are capable of causing primary lethal infections in humans, and the pandemic is now a global concern. The COVID-19 belongs to the beta coronavirus family encoding 29 proteins, of which four are structural, the Spike, Membrane, Envelope, and Nucleocapsid proteins. Here we have analyzed and compared the Membrane (M) and Envelope (E) proteins of COVID-19 and MERS with SARS and Bat viruses. The sequence analysis of conserved regions of both E and M proteins revealed that many regions of COVID-19 are similar to Bat and SARS viruses while the MERS virus showed variations. The essential binding motifs found in SARS appeared in COVID-19. Besides, the M protein of COVID-19 showed a distinct serine phosphorylation site in the C-terminal domain, which looked like a catalytic triad seen in serine proteases. A Dileucine motif occurred many times in the sequence of the M protein of all the four viruses compared. Concerning the structural part, the COVID-19 E protein showed more similarity to Bat while MERS shared similarity with the SARS virus. The M protein of both COVID-19 and MERS displayed variations in the structure. The interaction between M and E proteins was also studied to know the additional binding regions. Our study highlights the critical motifs and structural regions to be considered for further research to design better inhibitors for the infection caused by these viruses.
Insights
Coronaviruses like COVID-19 cause lethal infections. Comparing Membrane (M) and Envelope (E) proteins reveals similarities between COVID-19, SARS, and Bat viruses, aiding in inhibitor design.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Coronaviruses, including SARS, MERS, and COVID-19, pose significant global health threats.
- Structural proteins like Membrane (M) and Envelope (E) are crucial for viral function and pathogenesis.
- Understanding protein similarities and differences is key to developing effective antiviral strategies.
Purpose of the Study:
- To compare the Membrane (M) and Envelope (E) proteins of COVID-19 with those of MERS, SARS, and Bat coronaviruses.
- To identify conserved and variable regions, binding motifs, and structural features within these proteins.
- To explore potential interaction sites between M and E proteins for therapeutic target identification.
Main Methods:
- Sequence analysis of conserved regions in M and E proteins.
- Identification and comparison of essential binding motifs.
- Structural comparison of M and E proteins across different coronaviruses.
- Analysis of M protein phosphorylation sites and dileucine motifs.
Main Results:
- COVID-19 M and E proteins share significant sequence similarity with Bat and SARS viruses, unlike MERS.
- Essential binding motifs found in SARS are present in COVID-19.
- COVID-19 M protein exhibits a unique serine phosphorylation site; a dileucine motif is common across all viruses.
- Structural analysis shows COVID-19 E protein is more similar to Bat, while MERS E protein resembles SARS; M proteins show variations.
Conclusions:
- Comparative analysis of M and E proteins provides insights into coronavirus evolution and pathogenesis.
- Identified conserved motifs and structural features in COVID-19 M and E proteins are potential targets for antiviral drug development.
- Further research into M-E protein interactions may reveal novel therapeutic strategies against coronaviruses.
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