Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domain

Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domain

Blog Article

Summary: Omicron, as the emerging variant with enhanced vaccine tolerance, has sharply disrupted most therapeutic antibodies.Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) belongs to the subgenus Sarbecovirus, members of which share high sequence similarity.Herein, we report one sarbecovirus antibody, 5817, which has broad-spectrum neutralization capacity against SARS-CoV-2 variants of concern (VOCs) and SARS-CoV, as well as related bat and pangolin viruses.5817 can hardly compete with bg tuley six classes of receptor-binding-domain-targeted antibodies grouped by structural classifications.No obvious impairment in fox 985-24-100 reservoir shock the potency is detected against SARS-CoV-2 Omicron and subvariants.

The cryoelectron microscopy (cryo-EM) structure of neutralizing antibody 5817 in complex with Omicron spike reveals a highly conserved epitope, only existing at the receptor-binding domain (RBD) open state.Prophylactic and therapeutic administration of 5817 potently protects mice from SARS-CoV-2 Beta, Delta, Omicron, and SARS-CoV infection.This study reveals a highly conserved cryptic epitope targeted by a broad sarbecovirus neutralizing antibody, which would be beneficial to meet the potential threat of pre-emergent SARS-CoV-2 VOCs.