Addition of a single glycosylation site to hAPN blocks human coronavirus-229E receptor activity

Advances in Experimental Medicine and Biology

Volumn 494, Issue , 2001, Pages 199-204

  Wentworth, David E ^a   Holmes, Kathryn V ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MICROSOMAL AMINOPEPTIDASE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; CELL STRAIN BHK; CONFERENCE PAPER; CORONAVIRUS; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; REACTION ANALYSIS; RECEPTOR BLOCKING; RECEPTOR INTRINSIC ACTIVITY; SEQUENCE ANALYSIS; SEROTYPE; SIGNAL TRANSDUCTION; VIRUS CELL INTERACTION; VIRUS STRAIN;

CORONAVIRUS; HUMAN CORONAVIRUS 229E;

EID: 0035701332     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-1325-4_32     Document Type: Conference Paper

References (12)

1. Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site
2. Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV
3. Further characterization of aminopeptidase-N as a receptor for coronaviruses
4. Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N
5. Topology of microvillar membrance hydrolases of kidney and intestine
6. Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N
7. Involvement of aminopeptidase N (CD13) in infection of human neural cells by human coronavirus 229E
8. Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N
9. CD13 - Not just a marker in leukemia typing
10. Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup 1
11. Human aminopeptidase N is a receptor for human coronavirus 229E