Animal Husbandry and Feed Science ›› 2021, Vol. 42 ›› Issue (2): 1-6.doi: 10.12160/j.issn.1672-5190.2021.02.001

• Basic Research •     Next Articles

Prediction of Function and Structure of Porcine Aminopeptidase N by Using Bioinformatic Software

JIA Yan1, CAO Jin-shan1, WEI Zhan-yong2   

  1. 1. College of Veterinary Medicine,Inner Mongolia Agricultural University,Hohhot 010018,China;
    2. College of Veterinary Medicine,Henan Agricultural University,Zhengzhou 450046,China
  • Received:2020-11-19 Online:2021-03-30 Published:2021-04-16

Abstract: [Objective] To investigate the underlining molecular mechanism of porcine deltacoronavirus (PDCoV) invading the host cells, the structure and function of the protein that served as a specific receptor of PDCoV and encoded by the aminopeptidase N gene (pAPN) was bioinformatically analyzed. [Method] A variety of bioinformatic software was used to predict and assess the physical and chemical properties, hydrophilicity and hydrophobicity, signal peptide, transmembrane domain, glycosylation site,antigenic epitope, functional domain, and structural characteristics of pAPN protein. [Result] The total length of pAPN gene is 2 892 bp, which encodes 963 amino acids. Among them, the 35th~963th amino acids are the extramembrane protein region, which do not contain signal peptide but contain two typical functional domains. pAPN protein contains 23 glycosylation modification sites and 42 antigenic epitopes. The spatial structure of extracellular domain of pAPN protein is a dimer, and each monomer can be divided into four domains of Ⅰ~Ⅳ. [Conclusion] This study provides information for understanding the molecular mechanism of interactions between pAPN protein and various porcine enteric coronaviruses.

Key words: porcine aminopeptidase N, enteric coronaviruses, bioinformatic software, function, structure

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