SARS-CoV/SARS-CoV-2 Spike Glycoprotein RBD Chimeric Monoclonal Antibody (Clone D002)

Severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein, also known as the surface glycoprotein, is a viral structural protein encoded by the S gene in SARS-CoV RNA that contains the receptor binding domain (RBD).¹ SARS-CoV is a member of the Betacoronavirus genus of viruses and has an approximately 79% sequence identity with SARS-CoV-2, the causative agent of COVID-19.^2,3 SARS-CoV spike glycoprotein is a transmembrane glycoprotein that assembles into homotrimers on the virus surface and is composed of an N-terminal S1 subunit, which contains the receptor binding domain (RBD), and a C-terminal S2 subunit, which facilitates fusion between viral and host cell membranes.^4,5,6 The 193-amino acid RBD of the SARS-CoV spike protein is a target for neutralizing antibodies.^5,7 The SARS-CoV RBD, which spans amino acid residues 318 to 510, is 73% identical to that of SARS-CoV-2 and can bind to human angiotensin-converting enzyme 2 (ACE2), which is the host cell surface receptor for both SARS-CoV and SARS-CoV-2.^5,4,7,6 SARS-CoV is the causative agent of SARS, a primarily respiratory illness characterized by fever, cough, shortness of breath, and an approximately 10% fatality rate.³ Cayman's SARS-CoV/SARS-CoV-2 Spike Glycoprotein RBD Chimeric Monoclonal Antibody (Clone D002) is composed of human IgG1κ constant domains and variable regions from a mouse immunized with purified recombinant SARS-CoV spike glycoprotein RBD. It can be used for ELISA and flow cytometry (FC) applications, as well as microneutralization (MN) assays.

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4. Liu, Z., Xiao, X., Wei, X., et al. Composition and divergence of coronavirus spike proteins and host ACE2 receptors predict potential intermediate hosts of SARS-CoV-2. J. Med. Virol. 92(6), 595-601 (2020).

5. He, Y., Zhou, Y., Liu, S., et al. Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: Implication for developing subunit vaccine. Biochem. Biophys. Res. Commun. 324(2), 773-781 (2004).

6. Walls, A.C., Park, Y.-J., Tortorici, M.A., et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181(2), 281-292 (2020).

7. Tian, X., Li, C., Huang, A., et al. Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody. Emerg. Microbes Infect. 9(1), 382-385 (2020).