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Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
Open accessAbstract
The recognition and binding of cholesterol is an important feature of many eukaryotic, viral, and prokaryotic proteins, but the molecular details of such interactions are understood only for a few proteins. The pore-forming cholesterol-dependent cytolysins (CDCs) contribute to the pathogenic mechanisms of a large number of Gram-positive bacteria. Cholesterol dependence of the CDC mechanism is a hallmark of these toxins, yet the identity of the CDC cholesterol recognition motif has remained elusive. A detailed analysis of membrane interactive structures at the tip of perfringolysin O (PFO) domain 4 reveals that a threonine-leucine pair mediates CDC recognition of and binding to membrane cholesterol. This motif is conserved in all known CDCs and conservative changes in its sequence or order are not well tolerated. Thus, the Thr-Leu pair constitutes a common structural basis for mediating CDC-cholesterol recognition and binding, and defines a unique paradigm for membrane cholesterol recognition by surface-binding proteins.
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Citations
Cited by
Pore-forming toxins: ancient, but never really out of fashion
Peraro, M. D., & van der Goot, F. G. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2015.3 · Cited by 788
Listeriolysin O: the Swiss army knife of Listeria
Hamon, M. A., Ribet, D., Stavru, F., & Cossart, P. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.04.006 · Cited by 295
Orthogonal lipid sensors identify transbilayer asymmetry of plasma membrane cholesterol
Liu, S.-L., Sheng, R., Jung, J. H., Wang, L., Stec, E., O'Connor, M. J., Song, S., Bikkavilli, R. K., Winn, R. A., Lee, D., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2268 · Cited by 239
Cholesterol selectively activates canonical Wnt signalling over non-canonical Wnt signalling
Sheng, R., Kim, H., Lee, H., Xin, Y., Chen, Y., Tian, W., Cui, Y., Choi, J.-C., Doh, J., Han, J.-K., et al. (2014) · Nature Communications · doi:10.1038/ncomms5393 · Cited by 157
“We thus used the EGFP-tagged D434A mutant of the D4 domain, which has higher cholesterol affinity than the WT D4 domain 53 , as a cholesterol probe in this study.”
Sokolov, A., & Radhakrishnan, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.148254 · Cited by 105
Metadata
- Authors
- Farrand, A. J., LaChapelle, S., Hotze, E. M., Johnson, A. E., & Tweten, R. K.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-02-09
- Volume
- 107
- Issue
- 9
- Pages
- 4341-4346
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2007395394
- Cited by
- 208
- References
- 0
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- green
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- Farrand, A. J., LaChapelle, S., Hotze, E. M., Johnson, A. E., & Tweten, R. K. (2010). Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0911581107
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