Please use this identifier to cite or link to this item:
|標題:||Facilitative Production of an Antimicrobial Peptide Royalisin and Its Antibody via an Artificial Oil-Body System||作者:||Tseng, J.M.
|關鍵字:||royalisin;antimicrobial peptides;oleosin;artificial oil bodies;(AOBs);intein;insect defensin-a;escherichia-coli;antibacterial peptide;functional;expression;bodies;purification;proteins;immunity;oleosin;surface||Project:||Biotechnology Progress||期刊/報告no：:||Biotechnology Progress, Volume 27, Issue 1, Page(s) 153-161.||摘要:||
Royalisin found in the royal jelly of Apis mellifera is an antimicrobial peptide (AMP). It has a molecular weight of 5.5 kDa, which contains six cysteine residues. In this study, royalisin was overexpressed in Escherichia coli AD494 (DE3) as two oleosin-fusion proteins for preparation of its antibodies and functional purification. The recombinant royalisin, fused with oleosin central hydrophobic domain in both N-and C-termini, was reconstituted with triacylglycerol and phospholipids to form artificial oil bodies (AOBs). The AOBs were then purified to raise the antibodies. These antibodies could recognize both the native and recombinant royalisins, but not oleosin. Another oleosin-intein S-fusion protein was purified by AOBs system, and royalisin was subsequently released from the AOBs through self-splicing of the intein. The recombinant royalisin exhibited high antibacterial activity, which suggested that it was refolded to its functional structure. These results demonstrated that AOBs system is an efficient method to functionally express and purify small AMPs. In addition, it also provides a facile platform for the production of antibodies against small peptides. (C) 2010 American Institute of Chemical Engineers Biotechnol. Prog., 27: 153-161, 2011
|Appears in Collections:||期刊論文|
Show full item record
TAIR Related Article
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.