A structural analysis of the nsp9 protein from the coronavirus MERS CoV reveals a conserved RNA binding interface
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Published:2023-11-06
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Volume:
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ISSN:0887-3585
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Container-title:Proteins: Structure, Function, and Bioinformatics
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language:en
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Short-container-title:Proteins
Author:
Mani Gayathri1,
El‐Kamand Serene1,
Wang Bing2,
Baker David L.1,
Ataide Sandro F.3,
Artsimovitch Irina2,
Cubeddu Liza13,
Gamsjaeger Roland13ORCID
Affiliation:
1. School of Science Western Sydney University Penrith New South Wales Australia
2. Department of Microbiology The Ohio State University Columbus Ohio USA
3. School of Life and Environmental Sciences University of Sydney Camperdown New South Wales Australia
Abstract
AbstractMiddle East respiratory syndrome coronavirus (MERS CoV) and severe acute respiratory syndrome coronavirus 2 (SARS CoV‐2) are RNA viruses from the Betacoronavirus family that cause serious respiratory illness in humans. One of the conserved non‐structural proteins encoded for by the coronavirus family is non‐structural protein 9 (nsp9). Nsp9 plays an important role in the RNA capping process of the viral genome, where it is covalently linked to viral RNA (known as RNAylation) by the conserved viral polymerase, nsp12. Nsp9 also directly binds to RNA; we have recently revealed a distinct RNA recognition interface in the SARS CoV‐2 nsp9 by using a combination of nuclear magnetic resonance spectroscopy and biolayer interferometry. In this study, we have utilized a similar methodology to determine a structural model of RNA binding of the related MERS CoV. Based on these data, we uncover important similarities and differences to SARS CoV‐2 nsp9 and other coronavirus nsp9 proteins. Our findings that replacing key RNA binding residues in MERS CoV nsp9 affects RNAylation efficiency indicate that recognition of RNA may play a role in the capping process of the virus.
Funder
National Institutes of Health
Western Sydney University
Subject
Molecular Biology,Biochemistry,Structural Biology
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