Identification of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a binding protein for a 68-kDa <Emphasis Type="Italic">Bacillus thuringiensis</Emphasis> parasporal protein cytotoxic against leukaemic cells |
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| Authors: | Kanakeswary Krishnan Jeremy Er An Ker Shar Mariam Mohammed Vishna Devi Nadarajah |
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| Institution: | (1) Department of Pharmacy, Faculty of Medicine and Health Sciences, International Medical University, No 126 Jalan 19/155B Bukit Jalil, Kuala Lumpur, 57000, Malaysia;(2) School of Postgraduate Studies, Faculty of Medicine and Health Sciences, International Medical University, No 126 Jalan 19/155B Bukit Jalil, Kuala Lumpur, 57000, Malaysia;(3) Department of Human Biology, Faculty of Medicine and Health Sciences, International Medical University, No 126 Jalan 19/155B Bukit Jalil, Kuala Lumpur, 57000, Malaysia |
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| Abstract: | Background
Bacillus thuringiensis (Bt), an ubiquitous gram-positive spore-forming bacterium forms parasporal proteins during the stationary phase of its growth.
Recent findings of selective human cancer cell-killing activity in non-insecticidal Bt isolates resulted in a new category
of Bt parasporal protein called parasporin. However, little is known about the receptor molecules that bind parasporins and
the mechanism of anti-cancer activity. A Malaysian Bt isolate, designated Bt18 produces parasporal protein that exhibit preferential
cytotoxic activity for human leukaemic T cells (CEM-SS) but is non-cytotoxic to normal T cells or other cancer cell lines
such as human cervical cancer (HeLa), human breast cancer (MCF-7) and colon cancer (HT-29) suggesting properties similar to
parasporin. In this study we aim to identify the binding protein for Bt18 in human leukaemic T cells. |
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