Streptolysin O: Inhibition of the Conformational Change during Membrane Binding of the Monomer Prevents Oligomerization and Pore Formation
Author:
Affiliation:
1. Institute of Medical Microbiology, University of Mainz, Augustusplatz, D55101 Mainz, Germany, and Department of Microbiology, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, England
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi991678y
Reference42 articles.
1. Mechanism of membrane damage by streptolysin-O
2. Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O
3. Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae
4. Contribution of Individual Tryptophan Residues to the Structure and Activity of theta-Toxin (Perfringolysin O), A Cholesterol-Binding Cytolysin
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