Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein
Thomas G. Flower, Cosmo Z. Buffalo, Richard M. Hooy, Marc Allaire, Xuefeng Ren, James H. Hurley
Abstract
Significance The structure of the SARS-CoV-2 ORF8 protein reveals two novel intermolecular interfaces layered onto an ORF7 fold. One is mediated by a disulfide bond, the other is noncovalent, and both are novel with respect to SARS-CoV. The structural analysis here establishes a molecular framework for understanding the rapid evolution of ORF8, its contributions to COVID-19 pathogenesis, and the potential for its neutralization by antibodies.
Topics & Concepts
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)AntibodyDisulfide bondPathogenesisImmune systemEvasion (ethics)Coronavirus disease 2019 (COVID-19)NeutralizationIntermolecular force2019-20 coronavirus outbreakBiologyChemistryVirologyBiochemistryGeneticsImmunologyMedicineMoleculeDiseaseOutbreakInfectious disease (medical specialty)PathologyOrganic chemistrySARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections StudiesViral gastroenteritis research and epidemiology