Crystal structure of SARS-CoV-2 Orf9b in complex with human TOM70 suggests unusual virus-host interactions

Xiaopan Gao; Kaixiang Zhu; Bo Qin; Vincent Olieric; Meitian Wang; Sheng Cui

doi:10.1038/s41467-021-23118-8

Nature Communications (May 2021)

Crystal structure of SARS-CoV-2 Orf9b in complex with human TOM70 suggests unusual virus-host interactions

Xiaopan Gao,
Kaixiang Zhu,
Bo Qin,
Vincent Olieric,
Meitian Wang,
Sheng Cui

Affiliations

Xiaopan Gao: NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College
Kaixiang Zhu: NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College
Bo Qin: NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College
Vincent Olieric: Swiss Light Source Paul Scherrer Institut
Meitian Wang: Swiss Light Source Paul Scherrer Institut
Sheng Cui: NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College

DOI: https://doi.org/10.1038/s41467-021-23118-8
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 9

Abstract

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SARS-CoV-2 orf9b binds to the mitochondrial outer membrane protein TOM70 and has been linked to the suppression of interferon responses. Here, the authors characterize the interactions of SARS-CoV-2 orf9b and human TOM70 biochemically, and they determine the 2.2 Å crystal structure of the TOM70 cytosolic domain with a bound SARS-CoV-2 orf9b peptide.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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