Human Coronavirus 229E: Receptor Binding Domain and Neutralization by Soluble Receptor at 37°C

Jamie J. Breslin; Irene Mørk; Mary Smith; Lotte K. Vogel; Erin M. Hemmila; Aurelio Bonavia; Pierre J. Talbot; Hans Sjöström; Ove Norén; Kathryn V. Holmes

doi:10.1128/jvi.77.7.4435-4438.2003

Abstract

ABSTRACT Truncated human coronavirus HCoV-229E spike glycoproteins containing amino acids 407 to 547 bound to purified, soluble virus receptor, human aminopeptidase N (hAPN). Soluble hAPN neutralized the infectivity of HCoV-229E virions at 37°C, but not 4°C. Binding of hAPN may therefore trigger conformational changes in the viral spike protein at 37°C that facilitate virus entry.

Keywords

GlycoproteinCoronavirusBiologyInfectivityReceptorNeutralizationViral entrySpike ProteinVirologyVirusBiochemistryMolecular biologyCoronavirus disease 2019 (COVID-19)Viral replication

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Publication Info

Year: 2003
Type: article
Volume: 77
Issue: 7
Pages: 4435-4438
Citations: 74
Access: Closed

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APA Style

                            
                                
                                    Jamie J. Breslin, 
                                
                                    Irene Mørk, 
                                
                                    Mary Smith
                                
                                et al.
                            
                            (2003). 
                            Human Coronavirus 229E: Receptor Binding Domain and Neutralization by Soluble Receptor at 37°C. 
                            Journal of Virology
                            , 77
                            (7)
                            , 4435-4438.
                            https://doi.org/10.1128/jvi.77.7.4435-4438.2003
                        

Identifiers

DOI: 10.1128/jvi.77.7.4435-4438.2003