Structural characterization of SARS-CoV-2 dimeric ORF9b reveals potential fold-switching trigger mechanism.

ABSTRACT: The constant emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants indicates the evolution and adaptation of the virus. Enhanced innate immune evasion through increased expression of viral antagonist proteins, including ORF9b, contributes to the improved transmission of the Alpha variant; hence, more attention should be paid to these viral proteins. ORF9b is an accessory protein that suppresses innate immunity via a monomer conformation by binding to Tom70. Here, we solved the dimeric structure of SARS-CoV-2 ORF9b with a long hydrophobic tunnel containing a lipid molecule that is crucial for the dimeric conformation and determined the specific lipid ligands as monoglycerides by conducting a liquid chromatography with tandem mass spectrometry analysis, suggestin

SUBMITTER: Jin X 

PROVIDER: S-EPMC9527070 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature