ANPEP Antibody

1. Genetic ablation of APN expression had no effect on infectability by porcine epidemic diarrhea virus, demonstrating that APN is not essential for porcine epidemic diarrhea virus cell entry. PMID: 28363778
2. pAPN is not a functional receptor for porcine epidemic diarrhea virus, but promotes the infection of PEDV through its protease activity. PMID: 27449937
3. The C-terminal domain of the S1 domain of porcine epidemic diarrhea virus is bound to swine pAPN. PMID: 26907329
4. Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates. PMID: 26449746
5. SPC subdomain of APN plays a key role in cell entry of PEDV and its expression permits PEDV growth PMID: 26044794
6. Porcine epidemic diarrhea virus recognizes protein receptor aminopeptidase N from pig and human and sugar coreceptor N-acetylneuraminic acid. PMID: 25787280
7. These data demonstrate that pAPN, the cellular receptor for porcine epidemic diarrhea virus, mediates polarized virus infection. PMID: 25681796
8. It was concluded that the difference in F4 binding to ANPEP is due to modifications in its carbohydrate moieties. PMID: 24663207
9. The region aa 673-722 of the C subunit of porcine aminopeptidase N is indicated to play a key role in swine transmissible gastroenteritis virus binding. PMID: 22083718
10. The binding ability of four truncated porcine aminopeptidase N proteins to transmissible gastroenteritis virus (TGEV), a porcine coronavirus, was analyzed by ELISA and immunoblotting. PMID: 20643168
11. Aminoeptidase N is the major for cell entry system of porcine epidemic diarrhea virus infection. PMID: 20074871
12. results demonstrate that aminopeptidase N reduces basolateral Na(+)-K(+)-ATPase levels via ANG IV/AGTRIV signaling. This novel pathway may be important in renal adaptation to high salt PMID: 17634404

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KEGG: ssc:397520

STRING: 9823.ENSSSCP00000029051

UniGene: Ssc.820