Structural basis of pore formation by cholesterol-binding toxins.

Journal article

In this paper we describe reconstructions by electron cryo-microscopy of two oligomeric states of the pore-forming toxin pneumolysin. The results are interpreted by the fitting of atomic models of separated domains to the 3-dimensional electron density maps, revealing two steps in the mechanism of pore formation by the family of cholesterol-binding toxins. We briefly describe the observation of the toxin pore in model membranes and contrast the apparent mechanism of pneumolysin with that of other pore-forming toxins.

Authors: Gilbert, R; Jiménez, J; Chen, S; Andrew, P; Saibil, H

• Journal: International journal of medical microbiology : IJMM
• Volume: 290
• Issue: 4-5
• Pages: 389-394
• Publication date: 2000-10-01
• DOI: 10.1016/S1438-4221(00)80049-1
• EISSN: 1618-0607
• ISSN: 1438-4221
• Language: English
• Keywords: Protein Subunits; Protein Conformation; Microscopy, Electron; Cytotoxins; Bacterial Proteins; Bacterial Toxins; Streptolysins; Cholesterol; Hemolysin Proteins