To help their growth and spread, bacteria rely on virulence factors, many of which are toxic. One such factor is highly potent, as it attacks a key protein that 'chaperones' other proteins through their synthesis.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Paton, A. W. et al. Nature 443, 548–552 (2006).
Paton, A. W., Srimanote, P., Talbot, U. M., Wang, H. & Paton, J. C. J. Exp. Med. 200, 35–46 (2004).
Tarr, P. I., Gordon, C. A. & Chandler, W. L. Lancet 365, 1073–1086 (2005).
Sandvig, K. Toxicon 39, 1629–1635 (2001).
Rossetto, O. et al. Toxicon 39, 27–41 (2001).
Hendershot, L. M. Mt Sinai J. Med. 71, 289–297 (2004).
Luo, S., Mao, C., Lee, B. & Lee, A. S. Mol. Cell. Biol. 26, 5688–5697 (2006).
Baldari, T., Tonello, F., Paccani, S. & Montecucco, C. Trends Immunol. 27, 434–440 (2006).
Dong, D. et al. Cancer Res. 65, 5785–5791 (2005).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Montecucco, C., Molinari, M. Death of a chaperone. Nature 443, 511–512 (2006). https://doi.org/10.1038/443511a
Published:
Issue Date:
DOI: https://doi.org/10.1038/443511a