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

ABSTRACT: 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.

SUBMITTER: Sun D

PROVIDER: S-EPMC7087752 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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

Sun Dongbo D Shi Hongyan H Chen Jianfei J Guo Donghua D Liu Quan Q He Xianjing X Bao Jun J Wang Yunfeng Y Qiu Huaji H Feng Li L

Biotechnology letters 20111115 3

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) betwee ...[more]

PMID: 22083718

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