Warning: This is a preliminary report that has not been peer-reviewed. It should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information.

Double Lock of a Potent Human Monoclonal Antibody against SARS-CoV-2 (Preliminary Report)

Receptor recognition and subsequent membrane fusion are essential for the establishment of successful infection by SARS-CoV-2. Halting these steps can cure COVID-19. Here we have identified and characterized a potent human monoclonal antibody, HB27, that blocks SARS-CoV-2 attachment to its cellular receptor at sub-nM concentrations. Remarkably, HB27 can also prevent ...
SARS-CoV-2 membrane fusion. Consequently, a single dose of HB27 conferred effective protection against SARS-CoV-2 in two established mouse models. Rhesus macaques showed no obvious adverse events when administrated with 10-fold of effective dose of HB27. Cryo-EM studies on complex of SARS-CoV-2 trimeric S with HB27 Fab reveal that three Fab fragments work synergistically to occlude SARS-CoV-2 from binding to ACE2 receptor. Binding of the antibody also restrains any further conformational changes of the RBD, possibly interfering with progression from the prefusion to the postfusion stage. These results suggest that HB27 is a promising candidate for immuno-therapies against COVID-19.HighlightsO_LISARS-CoV-2 specific antibody, HB27, blocks viral receptor binding and membrane fusionC_LIO_LIHB27 confers prophylactic and therapeutic protection against SARS-CoV-2 in mice modelsC_LIO_LIRhesus macaques showed no adverse side effects when administered with HB27C_LIO_LICryo-EM studies suggest that HB27 sterically occludes SARS-CoV-2 from its receptorC_LI
Date: Nov. 25, 2020
Status: Preliminary Report
Download Curated Data For This Publication
226410
Switch View:
  • Interactions 3