The Cytotoxic Fimbrial Structural Subunit of Xenorhabdus nematophila Is a Pore-Forming Toxin

Author:

Banerjee Jyotirmoy1,Singh Jitendra21,Joshi Mohan Chandra21,Ghosh Shubhendu3,Banerjee Nirupama2

Affiliation:

1. Centre for Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India

2. International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India

3. Department of Biophysics, University of Delhi, New Delhi 110021, India

Abstract

ABSTRACT We have purified a fimbrial shaft protein (MrxA) of Xenorhabdus nematophila . The soluble monomeric protein lysed larval hemocytes of Helicoverpa armigera . Osmotic protection of the cells with polyethylene glycol suggested that the 17-kDa MrxA subunit makes pores in the target cell membrane. The internal diameter of the pores was estimated to be >2.9 nm. Electron microscopy confirmed the formation of pores by the fimbrial subunit. MrxA protein oligomerized in the presence of liposomes. Electrophysiological studies demonstrated that MrxA formed large, voltage-gated passive-diffusion channels in lipid bilayers.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference36 articles.

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