+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

The human coronavirus HCoV-229E S-protein structure and receptor binding

The human coronavirus HCoV-229E S-protein structure and receptor binding

Elife 8

The coronavirus S-protein mediates receptor binding and fusion of the viral and host cell membranes. In HCoV-229E, its receptor binding domain (RBD) shows extensive sequence variation but how S-protein function is maintained is not understood. Reported are the X-ray crystal structures of Class III-V RBDs in complex with human aminopeptidase N (hAPN), as well as the electron cryomicroscopy structure of the 229E S-protein. The structures show that common core interactions define the specificity for hAPN and that the peripheral RBD sequence variation is accommodated by loop plasticity. The results provide insight into immune evasion and the cross-species transmission of 229E and related coronaviruses. We also find that the 229E S-protein can expose a portion of its helical core to solvent. This is undoubtedly facilitated by hydrophilic subunit interfaces that we show are conserved among coronaviruses. These interfaces likely play a role in the S-protein conformational changes associated with membrane fusion.

Please choose payment method:

(PDF emailed within 1 workday: $29.90)

Accession: 069451336

Download citation: RISBibTeXText

PMID: 31650956

Related references

Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E. Journal of Virology 77(4): 2530-2538, 2003

A predicted receptor-binding and critical neutralizing domain in S protein of the novel human coronavirus HCoV-EMC. Journal of Infection 66(5): 464-466, 2013

Expression and identification of HcoV-229E coronavirus S1 protein in prokaryotic cell. 2008

Human coronavirus HCoV-229E enters susceptible cells via the endocytic pathway. Advances in Experimental Medicine and Biology 494: 193-198, 2001

Antibodies induced by receptor-binding domain in spike protein of SARS-CoV do not cross-neutralize the novel human coronavirus hCoV-EMC. Journal of Infection 67(4): 348-350, 2013

Acute life threatening event (ALTE) in an infant with human coronavirus HCoV-229E infection. Pediatric Pulmonology 42(4): 393-396, 2007

Characterization of HCoV-229E fusion core: implications for structure basis of coronavirus membrane fusion. Biochemical and Biophysical Research Communications 345(3): 1108-1115, 2006

Titration of human coronaviruses, HcoV-229E and HCoV-OC43, by an indirect immunoperoxidase assay. Methods in Molecular Biology 454: 93, 2008

Replication of human coronaviruses SARS-CoV, HCoV-NL63 and HCoV-229E is inhibited by the drug FK506. Virus Research 165(1): 112-117, 2012

False-positive results in a recombinant severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid enzyme-linked immunosorbent assay due to HCoV-OC43 and HCoV-229E rectified by Western blotting with recombinant SARS-CoV spike polypeptide. Journal of Clinical Microbiology 42(12): 5885-5888, 2004

Human Coronavirus 229E: Receptor Binding Domain and Neutralization by Soluble Receptor at 37C. Journal of Virology 77(7): 4435-4438, 2003

Human coronavirus 229E: Receptor binding domain and neutralization by soluble receptor at 37degreeC. Journal of Virology 77(7): 4435-4438, 2003

Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor. Biochimica et Biophysica Acta 1762(7): 693-703, 2006

Lack of association between infection with a novel human coronavirus (HCoV), HCoV-NH, and Kawasaki disease in Taiwan. Journal of Infectious Diseases 193(2): 283-286, 2005

Prokaryotic expression and characterization of two recombinant receptor-binding domain(RBD) proteins of human coronavirus NL63(HcoV-NL63). Bing du Xue Bao 29(2): 106-111, 2013