Identification of a putative cellular receptor 150 kDa polypeptide for porcine epidemic diarrhea virus in porcine enterocytes.
- Author:
Jin Sik OH
1
;
Dae Sub SONG
;
Bong Kyun PARK
Author Information
1. Department of Microbiology, Virology Lab, College of Veterinary Medicine and School of Agricultural Biotechnology, Seoul National University, Seoul 151-742, Korea. parkx026@snu.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
PEDV;
cellular receptor;
porcine aminopeptidase N
- MeSH:
Animals;
Antigens, CD13/*metabolism;
Cercopithecus aethiops;
Coronavirus/*metabolism;
Coronavirus Infections/*veterinary/virology;
Digestive System Diseases/metabolism/*veterinary/virology;
Enterocytes/enzymology/metabolism/virology;
Enzyme-Linked Immunosorbent Assay/veterinary;
Male;
Protein Binding;
Receptors, Virus/*metabolism;
Swine;
Swine Diseases/metabolism/*virology;
Vero Cells
- From:Journal of Veterinary Science
2003;4(3):269-275
- CountryRepublic of Korea
- Language:English
-
Abstract:
Porcine epidemic diarrhea virus (PEDV) causes an acute enteritis in pigs of all ages, often fatality for neonates. PEDV occupies an intermediate position between two well characterized members of the coronavirus group I, human coronavirus (HCoV-229E)and transmissible gastroenteritis virus (TGEV) which uses aminopeptidase N (APN), a 150 kDa protein, as their receptors. However, the receptor of the PEDV has not been identified yet. A virus overlay protein binding assay (VOPBA) was used to identify PEDV binding protein in permissive cells. The binding ability of PEDV to porcine APN (pAPN) and the effects of pAPN on infectivity of PEDV in Vero cells were also investigated. VOPBA identified a 150 kDa protein, as a putative PEDV receptor in enterocytes and swine testicle (ST) cells. Further the PEDV binding to pAPN was blocked by anti-pAPN and pAPN enhanced PEDV infectivity in Vero cells. In conclusion, these results suggested that pAPN may act as a receptor of PEDV.
