Structural highlights
Publication Abstract from PubMed
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 a 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 the 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.
Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.,Chen Y, Rajashankar KR, Yang Y, Agnihothram SS, Liu C, Lin YL, Baric RS, Li F J Virol. 2013 Jul 31. PMID:23903833[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen Y, Rajashankar KR, Yang Y, Agnihothram SS, Liu C, Lin YL, Baric RS, Li F. Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus. J Virol. 2013 Jul 31. PMID:23903833 doi:10.1128/JVI.01756-13
