Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms15216
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Funding
- National Natural Science Foundation of China [31470266, 31670164]
- Chinese Science and Technology Key Projects [2014ZX10004001, 2016YFC1200200-002]
- National Key Research and Development Program of China [2016YFD0500300]
- CAMS Innovation Fund for Medical Sciences [2016-12M-1-014]
- PUMC Youth Fund
- Fundamental Research Funds for the Central Universities [3332013118]
- Program for Changjiang Scholars and the Innovative Research Team in University [IRT13007]
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Human coronavirus (CoV) HKU1 is a pathogen causing acute respiratory illnesses and so far little is known about its biology. HKU1 virus uses its S1 subunit C-terminal domain (CTD) and not the N-terminal domain like other lineage A beta-CoVs to bind to its yet unknown human receptor. Here we present the crystal structure of HKU1 CTD at 1.9 angstrom resolution. The structure consists of three subdomains: core, insertion and subdomain-1 (SD-1). While the structure of the core and SD-1 subdomains of HKU1 are highly similar to those of other beta-CoVs, the insertion subdomain adopts a novel fold, which is largely invisible in the cryo-EM structure of the HKU1 S trimer. We identify five residues in the insertion subdomain that are critical for binding of neutralizing antibodies and two residues essential for receptor binding. Our study contributes to a better understanding of entry, immunity and evolution of CoV S proteins.
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