Peeking into a secret world of pore-forming toxins: membrane binding processes studied by surface plasmon resonance.

Pore-formation in cell membranes is used by many toxins to kill cells. It is usually a process involving multiple steps that are difficult to analyse at the molecular level. The use of surface plasmon resonance (SPR) has only recently been introduced into the study of pore-forming toxins (PFT). It can give useful data mostly on the first steps of the pore-forming process; the binding to the lipid membranes. In particular, it can make unique contributions to our knowledge of ligand specificity and the kinetics of binding. This mini-review summarizes some recent SPR studies of PFT.

[1]  Gregor Anderluh,et al.  Two-step Membrane Binding by Equinatoxin II, a Pore-forming Toxin from the Sea Anemone, Involves an Exposed Aromatic Cluster and a Flexible Helix* , 2002, The Journal of Biological Chemistry.

[2]  J. Lakey,et al.  A Novel Mechanism of Pore Formation , 2003, Journal of Biological Chemistry.

[3]  W. Cho,et al.  Membrane binding assays for peripheral proteins. , 2001, Analytical biochemistry.

[4]  Claus Duschl,et al.  Protein binding to supported lipid membranes: investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance , 1993 .

[5]  G. Puu,et al.  An approach for analysis of protein toxins based on thin films of lipid mixtures in an optical biosensor. , 2001, Analytical chemistry.

[6]  J. Lolkema,et al.  Membrane Topology and Insertion of Membrane Proteins: Search for Topogenic Signals , 2000, Microbiology and Molecular Biology Reviews.

[7]  Claus Duschl,et al.  A new class of thiolipids for the attachment of lipid bilayers on gold surfaces , 1994 .

[8]  J. Werkmeister,et al.  Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance. , 2001, Biochimica et biophysica acta.

[9]  G. Anderluh,et al.  Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria). , 2002, Toxicon : official journal of the International Society on Toxinology.

[10]  D. Myszka,et al.  Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. , 1997, Current opinion in biotechnology.

[11]  C R MacKenzie,et al.  Quantitative Analysis of Bacterial Toxin Affinity and Specificity for Glycolipid Receptors by Surface Plasmon Resonance* , 1997, The Journal of Biological Chemistry.

[12]  J H Lakey,et al.  Measuring protein-protein interactions. , 1998, Current opinion in structural biology.

[13]  J. Gouaux,et al.  Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore , 1996, Science.

[14]  Niv Papo,et al.  Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. , 2003, Biochemistry.

[15]  R C Stevens,et al.  Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. , 1996, Biochemistry.

[16]  D. Williams,et al.  Surface plasmon resonance analysis at a supported lipid monolayer. , 1998, Biochimica et biophysica acta.

[17]  Philippe Nizard,et al.  Does fusion of domains from unrelated proteins affect their folding pathways and the structural changes involved in their function? A case study with the diphtheria toxin T domain. , 2002, Protein engineering.

[18]  G. Anderluh,et al.  Cysteine-scanning mutagenesis of an eukaryotic pore-forming toxin from sea anemone: topology in lipid membranes. , 1999, European journal of biochemistry.

[19]  Horst Vogel,et al.  Stable self‐assembly of a protein engineering scaffold on gold surfaces , 2002, Protein science : a publication of the Protein Society.

[20]  H Nakajima,et al.  Kinetic Analysis of Binding between Shiga Toxin and Receptor Glycolipid Gb3Cer by Surface Plasmon Resonance* , 2001, The Journal of Biological Chemistry.

[21]  C. Pederzolli,et al.  Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes , 2005, The Journal of Membrane Biology.

[22]  D. Tsernoglou,et al.  Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states , 1994, Nature.

[23]  E. Gouaux.  Channel-forming toxins: tales of transformation. , 1997, Current opinion in structural biology.

[24]  J H Lakey,et al.  Emerging techniques for investigating molecular interactions at lipid membranes. , 1998, Biochimica et biophysica acta.