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

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...

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Detalles Bibliográficos
Autores principales: Sun, Dongbo, Shi, Hongyan, Chen, Jianfei, Guo, Donghua, Liu, Quan, He, Xianjing, Bao, Jun, Wang, Yunfeng, Qiu, Huaji, Feng, Li
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2011
Materias:
Original Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7087752/
https://www.ncbi.nlm.nih.gov/pubmed/22083718
http://dx.doi.org/10.1007/s10529-011-0795-1
Descripción
Sumario: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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10529-011-0795-1) contains supplementary material, which is available to authorized users.

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