Cross-neutralization of a SARS-CoV-2 antibody to a functionally conserved site is mediated by avidity

BioRxiv : the Preprint Server for Biology
Hejun LiuIan A. Wilson


Most antibodies isolated from COVID-19 patients are specific to SARS-CoV-2. COVA1-16 is a relatively rare antibody that also cross-neutralizes SARS-CoV. Here we determined a crystal structure of COVA1-16 Fab with the SARS-CoV-2 RBD, and a negative-stain EM reconstruction with the spike glycoprotein trimer, to elucidate the structural basis of its cross-reactivity. COVA1-16 binds a highly conserved epitope on the SARS-CoV-2 RBD, mainly through a long CDR H3, and competes with ACE2 binding due to steric hindrance rather than epitope overlap. COVA1-16 binds to a flexible up conformation of the RBD on the spike and relies on antibody avidity for neutralization. These findings, along with structural and functional rationale for the epitope conservation, provide a blueprint for development of more universal SARS-like coronavirus vaccines and therapies.


Oct 13, 2020·Nature·Christopher O BarnesPamela J Bjorkman
Apr 11, 2021·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·Saraiya TanmayKonstantinos Poulas

❮ Previous
Next ❯

Methods Mentioned

electron microscopy

Related Concepts

Related Feeds

BioRxiv & MedRxiv Preprints

BioRxiv and MedRxiv are the preprint servers for biology and health sciences respectively, operated by Cold Spring Harbor Laboratory. Here are the latest preprint articles (which are not peer-reviewed) from BioRxiv and MedRxiv.