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Expression and functional characterization of Helicobacter pylori catalase from baculovirus-infected insect cells
Conference paper   Peer reviewed

Expression and functional characterization of Helicobacter pylori catalase from baculovirus-infected insect cells

Suh-Chin Wu, Haimei Huang and Chih-Chien Lin
Enzyme and Microbial Technology, Vol.35(6-7), pp.482-487
01/12/2004

Abstract

Apoptosis Baculovirus Catalase Helicobacter pylori Insect cells
The catalase katA gene of Helicobacter pylori encodes an antioxidant enzyme to protect the bacteria from environmental toxic oxygen species. In this study, the baculovirus-insect cell expression system was used to express the full-length katA gene from the Taiwanese H. pylori TW-34 strain. Three lipidopteran insect cell lines (Sf9, Sf21, High5) were evaluated to produce the recombinant catalase (KatA) using serum-containing and serum-free media. Large-scale production and purification of the recombinant KatA protein was achieved in a 2-l bioreactor and through the use of immobilized metal affinity chromatography (IMAC). Human gastric carcinoma AGS cells were co-cultured with H. pylori and the presence of the purified KatA protein resulted in a significant decrease in the apoptotic bodies observed in AGS cells. Our present study is the first report to demonstrate the functionality of recombinant KatA protein expressed in baculovirus-infected insect cells to protect human gastric cell apoptosis against H. pylori insults. © 2004 Elsevier Inc. All rights reserved.

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