We are analyzing https://link.springer.com/article/10.1007/s00249-015-1106-x.

Title:
Measuring kinetic drivers of pneumolysin pore structure | European Biophysics Journal
Description:
Most membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins are thought to form pores in target membranes by assembling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by a mechanism dependent on protein concentration in which arc pores arise due to kinetic trapping of the pre-pore forms by the depletion of free protein subunits during oligomerization. Here we describe the use of a kinetic assay to study pore formation in red blood cells by the MACPF/CDC pneumolysin from Streptococcus pneumoniae. We show that cell lysis displays two kinds of dependence on protein concentration. At lower concentrations, it is dependent on the pre-pore to pore transition of arc oligomers, which we show to be a cooperative process. At higher concentrations, it is dependent on the amount of pneumolysin bound to the membrane and reflects the affinity of the protein for its receptor, cholesterol. A lag occurs before cell lysis begins; this is dependent on oligomerization of pneumolysin. Kinetic dissection of cell lysis by pneumolysin demonstrates the capacity of MACPF/CDCs to generate pore-forming oligomeric structures of variable size with, most likely, different functional roles in biology.
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Keywords {🔍}

pore, pubmed, article, google, scholar, gilbert, membrane, lysis, cas, rate, formation, cell, pneumolysin, concentration, prepore, lag, protein, pores, fig, proteins, toxin, phase, temperature, form, oligomerization, data, kinetic, macpfcdc, transition, dependence, poreforming, size, subunits, order, length, shown, model, attack, membranes, oligomers, arcs, concentrations, binding, biol, central, tweten, assembly, mechanism, anderluh, leung,

Topics {✒️}

beta-barrel-forming cholesterol-dependent cytolysin c-terminal membrane-binding domain perforin-mediated target-cell death article download pdf multimeric beta-barrel protein small-angle neutron scattering measuring kinetic drivers membrane attack complex/perforin curve-fitting program profit ce5500 double-beam spectrophotometer clostridium perfringens theta-toxin generate ring-shaped structures principal pore-forming subunit protease-nicked theta-toxin fluorescent dye-labeled proteins negative-stain electron microscopy perforin-mediated myocardial damage monomer-monomer interactions drive target antigen-presenting cells pore-forming protein involved macpf/cdc proteins bind protein molecule binds versatile pore-forming toxins lipid “flip-flop” macpf/cdc proteins—agents steady-state kinetic model real-time printer-plotter macpf/cdc pore size cholesterol-dependent cytolysin intermedilysin bacterial cholesterol-dependent cytolysin cytolytic pore-forming protein european economic area pore-forming proteins involves previously published images pre-pore oligomeric state perforin-related protein pleurotolysin pore-forming protein toxin macpf/cdc pore formation michaelis–menten equation study macpf/cdc proteins membrane attack complex protein subunits—monomers bind steady-state kinetics full size image partially toroidal structure purified pore-forming protein constitute pre-pore assemblies c8alpha-macpf reveals mechanism macpf/cdc pore activity ring-shaped pneumolysin oligomers

Questions {❓}

If rate phase A is governed by pre-pore to pore transition, and phase B by binding to the membrane, what governs the dependence of lag on toxin concentration?
If the pre-pore to pore transition governs rate phase A, what governs phase B?

Schema {🗺️}

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         headline:Measuring kinetic drivers of pneumolysin pore structure
         description:Most membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins are thought to form pores in target membranes by assembling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by a mechanism dependent on protein concentration in which arc pores arise due to kinetic trapping of the pre-pore forms by the depletion of free protein subunits during oligomerization. Here we describe the use of a kinetic assay to study pore formation in red blood cells by the MACPF/CDC pneumolysin from Streptococcus pneumoniae. We show that cell lysis displays two kinds of dependence on protein concentration. At lower concentrations, it is dependent on the pre-pore to pore transition of arc oligomers, which we show to be a cooperative process. At higher concentrations, it is dependent on the amount of pneumolysin bound to the membrane and reflects the affinity of the protein for its receptor, cholesterol. A lag occurs before cell lysis begins; this is dependent on oligomerization of pneumolysin. Kinetic dissection of cell lysis by pneumolysin demonstrates the capacity of MACPF/CDCs to generate pore-forming oligomeric structures of variable size with, most likely, different functional roles in biology.
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         dateModified:2016-02-23T00:00:00Z
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            Membrane Biology
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      headline:Measuring kinetic drivers of pneumolysin pore structure
      description:Most membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins are thought to form pores in target membranes by assembling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by a mechanism dependent on protein concentration in which arc pores arise due to kinetic trapping of the pre-pore forms by the depletion of free protein subunits during oligomerization. Here we describe the use of a kinetic assay to study pore formation in red blood cells by the MACPF/CDC pneumolysin from Streptococcus pneumoniae. We show that cell lysis displays two kinds of dependence on protein concentration. At lower concentrations, it is dependent on the pre-pore to pore transition of arc oligomers, which we show to be a cooperative process. At higher concentrations, it is dependent on the amount of pneumolysin bound to the membrane and reflects the affinity of the protein for its receptor, cholesterol. A lag occurs before cell lysis begins; this is dependent on oligomerization of pneumolysin. Kinetic dissection of cell lysis by pneumolysin demonstrates the capacity of MACPF/CDCs to generate pore-forming oligomeric structures of variable size with, most likely, different functional roles in biology.
      datePublished:2016-02-23T00:00:00Z
      dateModified:2016-02-23T00:00:00Z
      pageStart:365
      pageEnd:376
      license:http://creativecommons.org/licenses/by/4.0/
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         Pore formation
         Kinetics
         MACPF/CDC
         Toroidal pore
         Oligomerization
         Membrane structure
         Biochemistry
         general
         Biological and Medical Physics
         Biophysics
         Cell Biology
         Neurobiology
         Membrane Biology
         Nanotechnology
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