7COE

Crystal structure of Receptor binding domain of MERS-CoV and KNIH90-F1 Fab complex

Summary for 7COE

• Entry DOI: 10.2210/pdb7coe/pdb
• Descriptor: Heavy chain, Light chain, Spike glycoprotein, ... (6 entities in total)
• Functional Keywords: rbd, fab, complex, immune system
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 148495.68

Authors

Lee, J.Y.,Song, J.Y.,Lee, H.S.,Hong, E.,Jang, T.H. (deposition date: 2020-08-04, release date: 2021-08-04, Last modification date: 2023-11-29)

Primary citation

Jang, T.H.,Park, W.J.,Lee, H.,Woo, H.M.,Lee, S.Y.,Kim, K.C.,Kim, S.S.,Hong, E.,Song, J.,Lee, J.Y.
The structure of a novel antibody against the spike protein inhibits Middle East respiratory syndrome coronavirus infections.
Sci Rep, 12:1260-1260, 2022

PubMed Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) is a zoonotic virus, responsible for outbreaks of a severe respiratory illness in humans with a fatality rate of 30%. Currently, there are no vaccines or United States food and drug administration (FDA)-approved therapeutics for humans. The spike protein displayed on the surface of MERS-CoV functions in the attachment and fusion of virions to host cellular membranes and is the target of the host antibody response. Here, we provide a molecular method for neutralizing MERS-CoV through potent antibody-mediated targeting of the receptor-binding subdomain (RBD) of the spike protein. The structural characterization of the neutralizing antibody (KNIH90-F1) complexed with RBD using X-ray crystallography revealed three critical epitopes (D509, R511, and E513) in the RBD region of the spike protein. Further investigation of MERS-CoV mutants that escaped neutralization by the antibody supported the identification of these epitopes in the RBD region. The neutralizing activity of this antibody is solely provided by these specific molecular structures. This work should contribute to the development of vaccines or therapeutic antibodies for MERS-CoV.

PubMed: 35075213
DOI: 10.1038/s41598-022-05318-4

Experimental method

X-RAY DIFFRACTION (2.05 Å)