ArticleBiophysical journal2008
Oligomerization of membrane-bound diphtheria toxin (CRM197) facilitates a transition to the open form and deep insertion.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 15 citations in OpenAlex.
- Diphtheria toxin T-domain as a tool for inducing lipid vesicle fusion.Communications chemistry · 2025Article
- The sheet-to-helix transition is a potential gas-phase unfolding pathway for a multidomain protein CRMChinese chemical letters = Zhongguo hua xue kuai bao · 2025Article
- Membrane-Associated Conformation of HIV-1 Nef Investigated with Hydrogen Exchange Mass Spectrometry at a Langmuir Monolayer.Analytical chemistry · 2015Article
- APOL1 toxin, innate immunity, and kidney injury.Kidney international · 2015Review
- Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome P450 reductase (POR) in nanodiscs.The Journal of biological chemistry · 2012Article
- Continuous distribution model for the investigation of complex molecular architectures near interfaces with scattering techniques.Journal of applied physics · 2011Article
- Structure of functional Staphylococcus aureus alpha-hemolysin channels in tethered bilayer lipid membranes.Biophysical journal · 2009Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diphtheria toxin (DT) contains separate domains for receptor-specific binding, translocation, and enzymatic activity. After binding to cells, DT is taken up into endosome-like acidic compartments where the translocation domain inserts into the endosomal membrane and releases the catalytic domain into the cytosol. The process by which the catalytic domain is translocated across the endosomal membrane is known to involve pH-induced conformational changes; however, the molecular mechanisms are not yet understood, in large part due to the challenge of probing the conformation of the membrane-bound protein. In this work neutron reflection provided detailed conformational information for membrane-bound DT (CRM197) in situ. The data revealed that the bound toxin oligomerizes with increasing DT concentration and that the oligomeric form (and only the oligomeric form) undergoes a large extension into solution with decreasing pH that coincides with deep insertion of residues into the membrane. We interpret the large extension as a transition to the open form. These results thus indicate that as a function of bulk DT concentration, adsorbed DT passes from an inactive state with a monomeric dimension normal to the plane of the membrane to an active state with a dimeric dimension normal to the plane of the membrane.
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