Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD

• Published in: Cell reports (Cambridge) Vol. 28; no. 13; pp. 3395 - 3405.e6
• Main Authors: Wang, Nianshuang, Rosen, Osnat, Wang, Lingshu, Turner, Hannah L., Stevens, Laura J., Corbett, Kizzmekia S., Bowman, Charles A., Pallesen, Jesper, Shi, Wei, Zhang, Yi, Leung, Kwanyee, Kirchdoerfer, Robert N., Becker, Michelle M., Denison, Mark R., Chappell, James D., Ward, Andrew B., Graham, Barney S., McLellan, Jason S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 24.09.2019; Elsevier; The Author(s)
• Subjects: 60 APPLIED LIFE SCIENCES; coronavirus; crystal structure; DPP4; electron microscopy; Epitopes - metabolism; Humans; membrane fusion; MERS-CoV; Middle East Respiratory Syndrome Coronavirus - pathogenicity; receptor-binding; DPP4; crystal structure; coronavirus; electron microscopy; MERS-CoV; receptor-binding; membrane fusion

Middle East respiratory syndrome coronavirus (MERS-CoV) emerged into the human population in 2012 and has caused substantial morbidity and mortality. Potently neutralizing antibodies targeting the receptor-binding domain (RBD) on MERS-CoV spike (S) protein have been characterized, but much less is k...