Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1)using GST affinity purification and SILAC-based quantitative proteomics

Ameirika, . and Hong, Xi Sha and Hwang, Jung Shan * (2017) Identification of a target protein of Hydra actinoporin-like toxin-1 (HALT-1)using GST affinity purification and SILAC-based quantitative proteomics. Toxicon, 133. pp. 153-161. ISSN 0041 0101

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Abstract

Hydra actinoporin-like toxin-1 (HALT-1) is a 20.8 kDa pore-forming toxin isolated from Hydra magnipapillata. HALT-1 shares structural similarity with actinoporins, a family that is well known for its haemolytic and cytolytic activity. However, the precise pore-forming mechanism of HALT-1 remains an open question since little is known about the specific target binding for HALT-1. For this reason, a comprehensive proteomic analysis was performed using affinity purification and SILAC-based mass spectrometry to identify potential protein-protein interactions between mammalian HeLa cell surface proteins and HALT-1. A total of 4 mammalian proteins was identified, of which only folate receptor alpha was further verified by ELISA. Our preliminary results highlight an alternative-binding mode of HALT-1 to the human plasma membrane. This is the first evidence showing that HALT-1, an actinoporin-like protein,binds to a membrane protein, the folate receptor alpha. This study would advance our understanding of the molecular basis of toxicity of pore-forming toxins and provide new insights in the production of more potent inhibitors for the toxin-membrane receptor interactions.

Item Type: Article
Uncontrolled Keywords: actinoporin; cytolysin; folate receptor alpha; pore-forming protein; Hydra; protein-protein interactions
Subjects: Q Science > Q Science (General)
Q Science > QR Microbiology
Divisions: Sunway University > Research Centres > Sunway Institute for Healthcare Development
Depositing User: Dr Janaki Sinnasamy
Date Deposited: 31 May 2017 01:08
Last Modified: 31 May 2017 01:08
URI: http://eprints.sunway.edu.my/id/eprint/492

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