JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.00787-06v1
188/22/7957    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Banerjee, J.
Right arrow Articles by Banerjee, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Banerjee, J.
Right arrow Articles by Banerjee, N.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2006, p. 7957-7962, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00787-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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

Jyotirmoy Banerjee,3,{ddagger} Jitendra Singh,1,2,{ddagger} Mohan Chandra Joshi,1,2 Shubhendu Ghosh,3 and Nirupama Banerjee1*

International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India,1 Centre for Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India,2 Department of Biophysics, University of Delhi, New Delhi 110021, India3

Received 1 June 2006/ Accepted 16 August 2006

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.

* Corresponding author. Mailing address: International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India. Phone: 91-11-26181242. Fax: 91-11-26162316. E-mail: nirupama{at}icgeb.res.in.

{triangledown} Published ahead of print on 1 September 2006.

{ddagger} J.B. and J.S. contributed equally to this study.

Journal of Bacteriology, November 2006, p. 7957-7962, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00787-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2006 by the American Society for Microbiology. All rights reserved.