Giuseppe
Emeritus
[Source: Journal of Virology, full page: (LINK). Abstract, edited.]
Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus
Yaoqing Chen 1, Kanagalaghatta R. Rajashankar 2, Yang Yang 1, Sudhakar S. Agnihothram 3, Chang Liu 1, Yi-Lun Lin 1, Ralph S. Baric 3 and Fang Li1 *
Author Affiliations: 1 Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455, USA; 2 Department of Chemistry and Chemical Biology, Cornell University, NE-CAT, Advanced Photon Source, Argonne, IL 60439, USA; 3 Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27559, USA
Published ahead of print 31 July 2013, doi: 10.1128/JVI.01756-13. JVI.01756-13
ABSTRACT
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.
FOOTNOTES
*Correspondence should be sent to: Fang Li, Department of Pharmacology, University of Minnesota Medical School, 6-121 Jackson Hall, 321 Church St SE, Minneapolis, MN 55455, USA, Tel: +1 612-625-6149; Fax: +1 612-625-8408, E-mail: lifang@umn.edu
Copyright ? 2013, American Society for Microbiology. All Rights Reserved.
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Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus
Yaoqing Chen 1, Kanagalaghatta R. Rajashankar 2, Yang Yang 1, Sudhakar S. Agnihothram 3, Chang Liu 1, Yi-Lun Lin 1, Ralph S. Baric 3 and Fang Li1 *
Author Affiliations: 1 Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455, USA; 2 Department of Chemistry and Chemical Biology, Cornell University, NE-CAT, Advanced Photon Source, Argonne, IL 60439, USA; 3 Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27559, USA
Published ahead of print 31 July 2013, doi: 10.1128/JVI.01756-13. JVI.01756-13
ABSTRACT
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.
FOOTNOTES
*Correspondence should be sent to: Fang Li, Department of Pharmacology, University of Minnesota Medical School, 6-121 Jackson Hall, 321 Church St SE, Minneapolis, MN 55455, USA, Tel: +1 612-625-6149; Fax: +1 612-625-8408, E-mail: lifang@umn.edu
Copyright ? 2013, American Society for Microbiology. All Rights Reserved.
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