Mode of action of antimicrobial proteins, pore-forming toxins and biologically active peptides (Hypothesis)

Authors

  • O Schmidt Insect Molecular Biology, Faculty of Sciences (Waite Campus), University of Adelaide, Glen Osmond, SA 5064, Australia
  • M M Rahman Insect Molecular Biology, Faculty of Sciences (Waite Campus), University of Adelaide, Glen Osmond, SA 5064, Australia
  • G Ma Insect Molecular Biology, Faculty of Sciences (Waite Campus), University of Adelaide, Glen Osmond, SA 5064, Australia
  • U Theopold Department of Molecular Biology and Functional Genomics, Stockholm University, S-10691 Stockholm, Sweden
  • Y Sun The Biotechnology Research Center, Shanxi Academy of Agricultural Sciences, 64 N.Nongke, Taiyuan, Shanxi 030031, China
  • M Sarjan Faculty of Agriculture, University of Mataram, Lombok, Indonesia
  • M Fabbri Department of Experimental Oncology, European Institute of Oncology, I-20141 Milan, Italy
  • H Roberts Insect Molecular Biology, Faculty of Sciences (Waite Campus), University of Adelaide, Glen Osmond, SA 5064, Australia

Keywords:

antimicrobial peptides, pore-forming toxins, peptide hormones;, endocytosis, lipophorin, cholesterol, lipid rafts, channel formation, lectins

Abstract

Antimicrobial peptides and pore-forming toxins are important effectors in innate immune defence
reactions. But their mode of action, comprising the insertion into cholesterol-containing membranes is not known. Here we explore the mechanical implications of pore-formation by extracellular protein
assemblies that drive cellular uptake reactions by leverage-mediated (LM) processes, where oligomeric adhesion molecules bent membrane-receptors around ‘hinge’-like lipophorin particles. The
interactions of antimicrobial peptides, pore-forming toxins and biologically active proteins with LMassemblies provide a new paradigm for the configurational specificity and sterical selectivity of
biologically active peptides.

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Published

2005-07-01

Issue

Vol. 2 No. 2 (2005)

Section

Review