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Expression and functional analysis of porcine aminopeptidase N produced in prokaryotic expression system

Paper ID Volume ID Publish Year Pages File Format Full-Text
24155 43501 2009 6 PDF Available
Title
Expression and functional analysis of porcine aminopeptidase N produced in prokaryotic expression system
Abstract

Porcine aminopeptidase N (pAPN) is a cellular membrane protein and a functional receptor for porcine coronaviruses. Here, we describe the heterologous expression of pAPN without signal peptide in BL21(DE3)pLysS host cells. The Escherichia coli (E. coli) harboring the recombinant construct was efficiently induced to express the pAPN protein at a high level. The most optimal expression profile for pAPN expression was investigated. By inoculating a rabbit with the purified pAPN, a high tittered specific antibody was achieved. Biologically, the antibody reacted with either pAPN-expressing E. coli or native pAPN on the surface of swine testis cells. The pAPN and its specific antibody blocked transmissible gastroenteritis coronavirus infection in vitro. Furthermore, the localization of pAPN on the small intestine of swine was analyzed by immunohistochemistry.

Keywords
Porcine aminopeptidase N; Protein expression; Receptor; Biological activity
First Page Preview
Expression and functional analysis of porcine aminopeptidase N produced in prokaryotic expression system
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 141, Issues 1–2, 20 April 2009, Pages 91–96
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering