Alliance for Pandemic Preparedness

January 27, 2021

SARS-CoV-2 Recruits a Haem Metabolite to Evade Antibody Immunity



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A molecular study of SARS-CoV-2 found that the virus’s spike protein was able to bind to biliverdin and bilirubin, products of heme metabolism. The authors identified the phenomenon after observing a green pigment in protein precipitate of recombinant SARS-CoV-2 spike produced in human cell lines. Binding to biliverdin inhibited the ability of immune sera and a subset of monoclonal antibodies to neutralize the virus. The study findings suggest that the spike N-terminal domain (NTD), a key site for antibody binding, is a dynamic and flexible region, and that interaction with biliverdin can cause conformational changes in the NTD such that it may evade the immune response. Spike protein isolated from endemic coronaviruses (NL63 and OC43) did not have similar properties. 

Rosa et al. (Jan 26, 2021). SARS-CoV-2 Recruits a Haem Metabolite to Evade Antibody Immunity. Pre-print downloaded January 27 from