Pre-fusion structure of a human coronavirus spike protein

Robert N. Kirchdoerfer, Christopher A. Cottrell, Nianshuang Wang, Jesper Pallesen, Hadi M. Yassine, Hannah L. Turner, Kizzmekia S. Corbett, Barney S. Graham, Jason S. McLellan () and Andrew B. Ward ()
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Robert N. Kirchdoerfer: The Scripps Research Institute
Christopher A. Cottrell: The Scripps Research Institute
Nianshuang Wang: Geisel School of Medicine at Dartmouth
Jesper Pallesen: The Scripps Research Institute
Hadi M. Yassine: Viral Pathogenesis Laboratory, National Institute of Allergy and Infectious Diseases
Hannah L. Turner: The Scripps Research Institute
Kizzmekia S. Corbett: Viral Pathogenesis Laboratory, National Institute of Allergy and Infectious Diseases
Barney S. Graham: Viral Pathogenesis Laboratory, National Institute of Allergy and Infectious Diseases
Jason S. McLellan: Geisel School of Medicine at Dartmouth
Andrew B. Ward: The Scripps Research Institute

Nature, 2016, vol. 531, issue 7592, 118-121

Abstract: A 4.0 Å resolution cryo-electron microscopy structure of the pre-fusion form of the trimeric spike from the human coronavirus HKU1 provides insight into how the spike protein mediates host-cell attachment and membrane fusion.

Date: 2016
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DOI: 10.1038/nature17200

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