EPFL
 Biomedical Imaging GroupSTI
EPFL
  Publications
English only   BIG > Publications > Chaperone ClpB


 CONTENTS
 Home Page
 News & Events
 People
 Publications
 Tutorials and Reviews
 Research
 Demos
 Download Algorithms

 DOWNLOAD
 PDF
 Postscript
 All BibTeX References

Stressed Mycobacteria Use the Chaperone ClpB to Sequester Irreversibly Oxidized Proteins Asymmetrically Within and Between Cells

J. Vaubourgeix, G. Lin, N. Dhar, N. Chenouard, X. Jiang, H. Botella, T. Lupoli, O. Mariani, G. Yang, O. Ouerfelli, M. Unser, D. Schnappinger, J. McKinney, C. Nathan

Cell Host & Microbe, vol. 17, no. 2, pp. 178-190, February 11, 2015.



Mycobacterium tuberculosis (Mtb) defends itself against host immunity and chemotherapy at several levels, including the repair or degradation of irreversibly oxidized proteins (IOPs). To investigate how Mtb deals with IOPs that can neither be repaired nor degraded, we used new chemical and biochemical probes and improved image analysis algorithms for time-lapse microscopy to reveal a defense against stationary phase stress, oxidants, and antibiotics—the sequestration of IOPs into aggregates in association with the chaperone ClpB, followed by the asymmetric distribution of aggregates within bacteria and between their progeny. Progeny born with minimal IOPs grew faster and better survived a subsequent antibiotic stress than their IOP-burdened sibs. ClpB-deficient Mtb had a marked recovery defect from stationary phase or antibiotic exposure and survived poorly in mice. Treatment of tuberculosis might be assisted by drugs that cripple the pathway by which Mtb buffers, sequesters, and asymmetrically distributes IOPs.


@ARTICLE(http://bigwww.epfl.ch/publications/vaubourgeix1501.html,
AUTHOR="Vaubourgeix, J. and Lin, G. and Dhar, N. and Chenouard, N. and
        Jiang, X. and Botella, H. and Lupoli, T. and Mariani, O. and Yang,
        G. and Ouerfelli, O. and Unser, M. and Schnappinger, D. and
        McKinney, J. and Nathan, C.",
TITLE="Stressed Mycobacteria Use the Chaperone {ClpB} to Sequester
        Irreversibly Oxidized Proteins Asymmetrically Within and Between
        Cells",
JOURNAL="Cell Host \& Microbe",
YEAR="2015",
volume="17",
number="2",
pages="178--190",
month="February 11,",
note="")

© 2015 Elsevier. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from Elsevier.
This material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder.