The outbreak of a novel coronavirus (SARS-CoV-2) represents a pandemic threat that has been declared a public health emergency of international concern. The SARS-CoV-2 Spike Glycoprotein is a key target for vaccines, therapeutic antibodies, and diagnostics. Biologic Models designed this 3D printed protein model of the SARS-CoV-2 Spike Glycoprotein Antibody Complex 7KS9 to help scientists better visualize these targets.
Biologic Model of SARS-CoV-2 Spike Glycoprotein 3D printed and colored-coded to denote functional domains (NTD blue, RBD green, SD1, light tan, SD2 red-orange-yellow, FP cyan, RRAR brown), and the neutralizing human antibody (tinted purple). SCIENCE recently published the work of Daniel Wrapp crystalizing the current generation of the SARS-CoV-2 Spike Glycoprotein, 2019-nCoV-2. Following the illustrations and supplemental materials describing each domain by amino acid sequence, a series of 3D models were generated for interactive exploration and 3D printing.
SARS-CoV-2 Spike Glycoprotein Antibody Complex 7KS9
Like SARS-CoV-1, neutralization of the Spike Receptor Binding Domain (RBD: green) requires antibodies to achieve sufficient affinity for the RBD to initiate conformation change of the Presfusion Spike (6VXX) from its RBD-down state to its RBD-up state. Here we see how this potent neutralizing antibody binds the RBD motif in a very similar way that previous antibodies targeted SARS-CoV-1. Explore the antibody interactions with the RBD motif below.
Biologic Explorer: 7KS9
To better understand the structural relationship of the domains within the Spike Glycoprotein, a protein dataset 7KS9 has been colorized to match our 3d printed model. Explore each domain below after “Initializing” the dataset.
Biologic Model of SARS-CoV-2 Spike Glycoprotein bound to a neutralizing human monoclonal antibody is created from PDB dataset 7KS9 and 3D printed in Full-color Sandstone or Plastic.
Explore More SARS-CoV-2 Biologic Models
Learn more about the SARS-CoV-2 Spike Glycoprotein and explore different datasets that capture its interactions with different proteins and molecules: Learn More