Journal
ANNUAL REVIEW OF MICROBIOLOGY, VOL 69
Volume 69, Issue -, Pages 323-340Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-micro-091014-104233
Keywords
perfringolysin O; streptolysin O; sterol; CD59; intermedilysin; beta-barrel
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Funding
- NIAID NIH HHS [1R01 AI037657, R01 AI037657] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI037657] Funding Source: NIH RePORTER
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The mechanism by which the cholesterol-dependent cytolysins (CDCs) assemble their giant beta-barrel pore in cholesterol-rich membranes has been the subject of intense study in the past two decades. A combination of structural, biophysical, and biochemical analyses has revealed deep insights into the series of complex and highly choreographed secondary and tertiary structural transitions that the CDCs undergo to assemble their beta-barrel pore in eukaryotic membranes. Our knowledge of the molecular details of these dramatic structural changes in CDCs has transformed our understanding of how giant pore complexes are assembled and has been critical to our understanding of the mechanisms of other important classes of pore-forming toxins and proteins across the kingdoms of life. Finally, there are tantalizing hints that the CDC pore-forming mechanism is more sophisticated than previously imagined and that some CDCs are employed in pore-independent processes.
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