+ 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

Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N



Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N



Journal of General Virology 78: 2795-2802



Aminopeptidase N (APN) is the major cell surface receptor for group I coronaviruses. In this study, we have isolated and characterized a feline APN cDNA and shown that the transfection of human embryonic kidney cells with this cDNA renders them susceptible to infection with the feline coronavirus feline infectious peritonitis virus, the human coronavirus (HCV) 229E and the porcine coronavirus porcine transmissible gastroenteritis virus. By using chimeric APN genes, assembled from porcine and feline sequences, we have shown that, analogously to the human APN protein, a region within the amino-terminal part of the feline APN protein (encompassing amino acids 132-295) is essential for its HCV 229E receptor function. Furthermore, by comparing the relevant feline, human and porcine APN sequences, we were able to identify a hypervariable stretch of eight amino acids that are more closely related in the feline and human APN proteins than in the porcine APN molecule. Using PCR-directed mutagenesis, we converted this stretch of amino acids within the porcine APN molecule to the corresponding residues of the human APN molecule. These changes were sufficient to convert porcine APN into a functional receptor for HCV 229E and thus define a small number of residues that are critically important for the HCV 229E receptor function of human APN.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 008809994

Download citation: RISBibTeXText

PMID: 9367365


Related references

Identification of six new polymorphisms in the human coronavirus 229E receptor gene (aminopeptidase N/CD13). International Journal of Infectious Diseases 8(4): 217-222, 2004

Human aminopeptidase n is a receptor for human coronavirus 229e. Nature (London) 357(6377): 420-422, 1992

Involvement of aminopeptidase N (CD13) in infection of human neural cells by human coronavirus 229E. Journal of Virology 72(8): 6511-6519, 1998

Cells of human aminopeptidase N (CD13) transgenic mice are infected by human coronavirus-229E in vitro, but not in vivo. Virology 335(2): 185-197, 2005

Identification of residues in the receptor-binding domain (RBD) of the spike protein of human coronavirus NL63 that are critical for the RBD-ACE2 receptor interaction. Journal of General Virology 89(Pt 4): 1015-1024, 2008

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

Identification and characterization of a novel alpaca respiratory coronavirus most closely related to the human coronavirus 229E. Viruses 4(12): 3689-3700, 2012

Antigenic studies on coronavirus. I. Identification of the structural antigens of human coronavirus, strain 229E. Canadian Journal of Microbiology 27(3): 334-342, 1981

Antigenic studies on coronavirus 1. identification of the structural antigens of human coronavirus strain 229e. Canadian Journal of Microbiology 27(3): 334-342, 1981

Coronavirus isolates SK and SD from multiple sclerosis patients are serologically related to murine coronaviruses A59 and JHM and human coronavirus OC43, but not to human coronavirus 229E. Journal of Virology 38(1): 231-238, 1981

Characteristics of Australian human enteric coronavirus-like particles: comparison with human respiratory coronavirus 229E and duodenal brush border vesicles. Archives of Virology 97(3-4): 309-323, 1987

Characterization of the human coronavirus 229E (HCV 229E) gene 1. Advances in Experimental Medicine and Biology 342: 75-79, 1993

Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor. Journal of Biological Chemistry 274(39): 27642-27650, 1999

Characterization of functional domains in the human coronavirus HCV 229E receptor. Journal of General Virology 77: 2515-2521, 1996

A comprehensive structure-function map of the intracellular surface of the human C5a receptor. I. Identification of critical residues. Journal of Biological Chemistry 282(5): 3105-3121, 2007