Bacterial expression of larval peritrophins of Chryosomya bezziana

Three candidate antigens, Chrysomya bezziana peritrophin-48, Chrysomya bezziana peritrophin-15 and Chrysomya bezziana peritrophin-42, were prepared for recombinant protein production in Escherichia coli using a variety of expression vectors. Cb peritrophin-48 was expressed as a recombinant protein p...

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Bibliographic Details
Main Authors: Tony Voucoloco, Sri Muharsini, Florentina Supriyanti, Gene Wijffels
Format: Article
Language:English
Published: Pusat Penelitian dan Pengembangan Peternakan 2000-10-01
Series:Jurnal Ilmu Ternak dan Veteriner
Subjects:
GST
Online Access:http://medpub.litbang.pertanian.go.id/index.php/jitv/article/view/196/196
Description
Summary:Three candidate antigens, Chrysomya bezziana peritrophin-48, Chrysomya bezziana peritrophin-15 and Chrysomya bezziana peritrophin-42, were prepared for recombinant protein production in Escherichia coli using a variety of expression vectors. Cb peritrophin-48 was expressed as a recombinant protein possessing a carboxy-terminal hexaHis tag. Cb peritrophin-15 was expressed as both a glutathione S-transferase fusion protein and as an amino-terminal hexaHis tagged protein. The glutathione Stransferase Cb peritrophin-15 construct produced a heterogeneous group of fusion proteins. Cb peritrophin-42 was also expressed as an amino-terminal hexaHis tagged protein. The two putative domains of Cb peritrophin-42 were also separately expressed, again with amino-terminal hexaHis tags. Cultures of the hexaHis constructs Cb peritrophin-48, -15 and –42 were demonstrated to be useful for the production and purification of these protein antigens and were scaled-up for vaccine trials and protein characterization studies.
ISSN:0853-7380
2252-696X