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Cryo-EM and SPR Analysis of SARS-CoV-2 Spike Protein Neutralization by Cayman Antibody Complex
Case Study
Overview:
Cayman has made a SARS-CoV-2 (human) neutralizing recombinant antibody which disrupts the S1 RBD-ACE2 interaction.
Surface plasmon resonance (SPR) was used to evaluate the recombinant neutralizing antibody's ability to block binding of SARS-CoV-2 S1 receptor binding domain (RBD) variants to human angiotensin-converting enzyme 2 (hACE2).
Cryo-electron microscopy (cryo-EM) single-particle analysis was used to determine the structure of intrinsically difficult-to-crystallize, >0.5 MDa SARS-CoV-2 spike:Fab complex.
This case study shows the structure and conformational analysis of the SARS-CoV-2 spike glycoprotein trimer in complex with a Fab derived from a recombinant SARS-CoV-2 neutralizing antibody. Cayman's engineered recombinant antibody could effectively block the interaction of hACE2 with S1 RBD wild-type and Alpha variants better than that with the Beta variant.
These structural results from cryo-EM and SPR studies could aid in the development of vaccines and therapeutics for the SARS-CoV-2 variants.
To cite this case study: Assar, Z., Muzzarelli, K., Drulyte, I., et al. Cryo-EM and SPR Analysis of SARS-CoV-2 Spike Protein Neutralization by Cayman Antibody Complex. Case Study: Structural Biology Services, Cayman Chemical (2021).
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