Virus-binding activity of the truncated C subunit of porcine aminopeptidase N expressed in Escherichia coli

• Published in: Biotechnology letters Vol. 34; no. 3; pp. 533 - 539
• Main Authors: Sun, Dongbo, Shi, Hongyan, Chen, Jianfei, Guo, Donghua, Liu, Quan, He, Xianjing, Bao, Jun, Wang, Yunfeng, Qiu, Huaji, Feng, Li
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer-Verlag 01.03.2012; Springer Netherlands; Springer; Springer Nature B.V
• Subjects: Animals; Antibodies; Applied Microbiology; Binding; Biochemistry; Biological and medical sciences; Biomedical and Life Sciences; Biotechnology; Blotting, Western; CD13 Antigens - genetics; CD13 Antigens - metabolism; E coli; ELISA; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Gastroenteritis; Gastroenterology; Hogs; Life Sciences; membrane alanyl aminopeptidase; Microbiology; Original Research Paper; Peptides; Proteins; Receptors, Virus - genetics; Receptors, Virus - metabolism; Recognition; Recombinant; recombinant proteins; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Swine; transmissible gastroenteritis; Transmissible gastroenteritis virus; Transmissible gastroenteritis virus - physiology; Virus Attachment; Viruses; Western blotting; Porcine aminopeptidase N; Swine transmissible gastroenteritis virus; C subunit; Gastroenteritis virus; Virus-binding activity; Enzyme; Aminopeptidases; Escherichia coli; Gastroenteritis; Subunit; Pig; Virus; Peptidases; Vertebrata; Mammalia; Swine; Bacteria; Hydrolases; Artiodactyla; Ungulata; Enterobacteriaceae; Membrane alanyl aminopeptidase
• ISSN: 0141-5492; 1573-6776
• DOI: 10.1007/s10529-011-0795-1

Seven overlapping truncated forms of the C subunit of porcine aminopeptidase N (pAPN-C) were expressed in Escherichia coli. By western blotting and ELISA test, all recombinant proteins were recognized by the antibody against native porcine aminopeptidase N. Recombinant proteins, rpAPN-C2 (aa 623–722) and rpAPN-C3 (aa 673–772), had the highest binding activity with swine transmissible gastroenteritis virus among the truncated pAPN-C recombinant proteins. The overlapping region (aa 673–722) between rpAPN-C2 and rpAPN-C3 is indicated to play a key role in viral binding.