Recombinant protein of the receptor binding domain (RBD), Mutant (L452R-T478K) of SARS-CoV-2 (COVID-2019) Spike S1 from Wuhan pneumonia virus with C-terminal His/GFP-Tag. The mutations L452R-T478K are characteristic for the fast spreading SARS-CoV-2 virus variants B.1.617 emerged in India. These mutations are affecting the receptor binding domain (RBD) of the spike protein, which the virus uses to bind to human cells receptors and enter them. Due to the mutations, the virus is allowed to bind with higher affinity to human ACE2 receptor which results in increased transmissibility of the SARS-CoV-2 virus.
“In our COVID-19 projects, we have had very good experience with the SARS-CoV-2 proteins produced by trenzyme: rapid and reliable production of the functional proteins from different cell lines continued to provide first-class support for our projects.”
Dr. Peter Rauch CANDOR Bioscience GmbH, Wangen, Germany
The spike (S) glycoprotein of coronaviruses is essential for binding of the virus to the host cell at the beginning of the infection process. The target protein is also a major immunogen and a possible target for entry inhibitors. The SARS-CoV-2 spike (S) protein is a large type I transmembrane protein composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain (RBD) responsible for binding to the host cell receptor angiotensin-converting enzyme 2 (ACE2). Several mutants of the spike protein are known. A new SARS-CoV-2 lineage called B.1.617, exhibits 13 mutations. Compared to the previously circulating variants, the mutations L452R and T478K of the SARS-CoV-2 Spike S1 (RBD) may cause a stronger affinity of the spike protein to hACE2 and also conferring an increasing ability to evade the hosts’ immune system.
Binding of Delta spike RBD variant to the membrane of ACE2 overexpressing cells
Binding of Delta spike RBD-GFP variant to wild-type HEK293 cells or those overexpressing ACE2 at different RBD concentrations (0.2, 1 and 5 µg/ml) after a labeling of 5 minutes. Data provided by Kovacs T., Nagy P., Panyi G. and Zakany F., Department of Biophysics and Cell Biology, University of Debrecen, Hungary