Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.
Publication Type:Journal Article
Source:J Virol, Volume 87, Issue 19, p.10777-83 (2013)
Keywords:Amino Acid Sequence, Coronavirus, Crystallography, X-Ray, Dipeptidyl Peptidase 4, Host-Pathogen Interactions, Humans, Leukemia Virus, Murine, Middle East, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Syndrome, Viral Proteins
<p>The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. </p>