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Journal of Virology, April 2003, p. 4435-4438, Vol. 77, No. 7
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.7.4435-4438.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Human Coronavirus 229E: Receptor Binding Domain and Neutralization by Soluble Receptor at 37°C
Jamie J. Breslin,1 Irene Mørk,2 M. K. Smith,1 Lotte K. Vogel,2 Erin M. Hemmila,1 Aurelio Bonavia,1 Pierre J. Talbot,3 Hans Sjöström,2 Ove Norén,2,
and Kathryn V. Holmes1*
Department of Microbiology, University of Colorado Health Sciences Center, Denver, Colorado 80262,1
Department of Medical Biochemistry and Genetics, University of Copenhagen, Copenhagen, Denmark,2
INRS-Institut Armand-Frappier, University of Quebec, Laval, Canada3
Received 18 September 2002/
Accepted 27 December 2002
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.
* Corresponding author. Mailing address: Department of Microbiology, School of Medicine, University of Colorado Health Sciences Center, Campus Box B-175, 4200 East 9th Ave., Denver, CO 80262. Phone: (303) 315-7329. Fax: (303) 315-6785. E-mail:
kathryn.holmes{at}uchsc.edu.
Deceased.
Journal of Virology, April 2003, p. 4435-4438, Vol. 77, No. 7
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.7.4435-4438.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
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