ArticleMolecular microbiology2014
A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- Central carbon flux controls growth/damage balance for Streptococcus pyogenes.PLoS pathogens · 2023Article
- Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection.Communications biology · 2023Article
- Identification of the pore-forming and binding domains of the Sneathia vaginalis cytopathogenic toxin A.PloS one · 2023Article
- Structure of the Streptococcus pyogenes NADJournal of bacteriology · 2022Article
- Article
- Article
- Changes in the asymmetric distribution of cholesterol in the plasma membrane influence streptolysin O pore formation.Scientific reports · 2019Article
- Host and bacterial proteases influence biofilm formation and virulence in a murine model of enterococcal catheter-associated urinary tract infection.NPJ biofilms and microbiomes · 2017Article
- Article
- Dual modes of membrane binding direct pore formation by Streptolysin O.Molecular microbiology · 2015Article
- The Unique Molecular Choreography of Giant Pore Formation by the Cholesterol-Dependent Cytolysins of Gram-Positive Bacteria.Annual review of microbiology · 2015Review
- The cholesterol-dependent cytolysins pneumolysin and streptolysin O require binding to red blood cell glycans for hemolytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
3 authors.
Funding
Abstract
Cytolysin-mediated translocation (CMT), performed by Streptococcus pyogenes, utilizes the cholesterol-dependent cytolysin Streptolysin O (SLO) to translocate the NAD(+) -glycohydrolase (SPN) into the host cell during infection. SLO is required for CMT and can accomplish this activity without pore formation, but the details of SLO's interaction with the membrane preceding SPN translocation are unknown. Analysis of binding domain mutants of SLO and binding domain swaps between SLO and homologous cholesterol-dependent cytolysins revealed that membrane binding by SLO is necessary but not sufficient for CMT, demonstrating a specific requirement for SLO in this process. Despite being the only known receptor for SLO, this membrane interaction does not require cholesterol. Depletion of cholesterol from host membranes and mutation of SLO's cholesterol recognition motif abolished pore formation but did not inhibit membrane binding or CMT. Surprisingly, SLO requires the coexpression and membrane localization of SPN to achieve cholesterol-insensitive membrane binding; in the absence of SPN, SLO's binding is characteristically cholesterol-dependent. SPN's membrane localization also requires SLO, suggesting a co-dependent, cholesterol-insensitive mechanism of membrane binding occurs, resulting in SPN translocation.
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