Structural basis of RNA cap modification by SARS-CoV-2

Specific non-structural proteins (nsp) of SARS coronaviruses are involved in methylation of virally encoded mRNAs to mimic cellular mRNAs for protection against host innate immune restriction. Here, the authors present a high resolution structure of SARS-CoV-2 nsp16/nsp10 ternary complex in the pres...

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Main Authors:	Thiruselvam Viswanathan, Shailee Arya, Siu-Hong Chan, Shan Qi, Nan Dai, Anurag Misra, Jun-Gyu Park, Fatai Oladunni, Dmytro Kovalskyy, Robert A. Hromas, Luis Martinez-Sobrido, Yogesh K. Gupta
Format:	Article
Language:	English
Published:	Nature Publishing Group 2020-07-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-020-17496-8

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spelling	doaj-1a2c5dcfc62842e8b013e549e88fbd222021-07-25T11:40:48ZengNature Publishing GroupNature Communications2041-17232020-07-011111710.1038/s41467-020-17496-8Structural basis of RNA cap modification by SARS-CoV-2Thiruselvam Viswanathan0Shailee Arya1Siu-Hong Chan2Shan Qi3Nan Dai4Anurag Misra5Jun-Gyu Park6Fatai Oladunni7Dmytro Kovalskyy8Robert A. Hromas9Luis Martinez-Sobrido10Yogesh K. Gupta11Greehey Children’s Cancer Research Institute, University of Texas Health at San AntonioGreehey Children’s Cancer Research Institute, University of Texas Health at San AntonioNew England BiolabsGreehey Children’s Cancer Research Institute, University of Texas Health at San AntonioNew England BiolabsGreehey Children’s Cancer Research Institute, University of Texas Health at San AntonioTexas Biomedical Research InstituteTexas Biomedical Research InstituteGreehey Children’s Cancer Research Institute, University of Texas Health at San AntonioDivision of Hematology and Oncology, Department of Medicine, University of Texas Health at San AntonioTexas Biomedical Research InstituteGreehey Children’s Cancer Research Institute, University of Texas Health at San AntonioSpecific non-structural proteins (nsp) of SARS coronaviruses are involved in methylation of virally encoded mRNAs to mimic cellular mRNAs for protection against host innate immune restriction. Here, the authors present a high resolution structure of SARS-CoV-2 nsp16/nsp10 ternary complex in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine, revealing unique ligand-binding sites that may represent alternative targets for antiviral development.https://doi.org/10.1038/s41467-020-17496-8
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Thiruselvam Viswanathan Shailee Arya Siu-Hong Chan Shan Qi Nan Dai Anurag Misra Jun-Gyu Park Fatai Oladunni Dmytro Kovalskyy Robert A. Hromas Luis Martinez-Sobrido Yogesh K. Gupta
spellingShingle	Thiruselvam Viswanathan Shailee Arya Siu-Hong Chan Shan Qi Nan Dai Anurag Misra Jun-Gyu Park Fatai Oladunni Dmytro Kovalskyy Robert A. Hromas Luis Martinez-Sobrido Yogesh K. Gupta Structural basis of RNA cap modification by SARS-CoV-2 Nature Communications
author_facet	Thiruselvam Viswanathan Shailee Arya Siu-Hong Chan Shan Qi Nan Dai Anurag Misra Jun-Gyu Park Fatai Oladunni Dmytro Kovalskyy Robert A. Hromas Luis Martinez-Sobrido Yogesh K. Gupta
author_sort	Thiruselvam Viswanathan
title	Structural basis of RNA cap modification by SARS-CoV-2
title_short	Structural basis of RNA cap modification by SARS-CoV-2
title_full	Structural basis of RNA cap modification by SARS-CoV-2
title_fullStr	Structural basis of RNA cap modification by SARS-CoV-2
title_full_unstemmed	Structural basis of RNA cap modification by SARS-CoV-2
title_sort	structural basis of rna cap modification by sars-cov-2
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2020-07-01
description	Specific non-structural proteins (nsp) of SARS coronaviruses are involved in methylation of virally encoded mRNAs to mimic cellular mRNAs for protection against host innate immune restriction. Here, the authors present a high resolution structure of SARS-CoV-2 nsp16/nsp10 ternary complex in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine, revealing unique ligand-binding sites that may represent alternative targets for antiviral development.
url	https://doi.org/10.1038/s41467-020-17496-8
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Structural basis of RNA cap modification by SARS-CoV-2

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