Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
| Autor: | Stefan Wieser, Michael C. Aichinger, Mario Brameshuber, Julian Weghuber, Gerhard J. Schütz, Karl Lohner, Tamás Henics, Josef Madl, Andreas Horner, Verena Ruprecht, Siegfried Reipert, Birgit Plochberger |
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| Rok vydání: | 2011 |
| Předmět: |
Plasma membrane accumulation
KLK Membrane lipids Biophysics Peptide Sialic acids Biology Endocytosis Biochemistry Article Hydrophobic effect Membrane Lipids 03 medical and health sciences chemistry.chemical_compound CAMPs Cations Animals Humans Amino Acid Sequence Peptide sequence Cells Cultured 030304 developmental biology chemistry.chemical_classification 0303 health sciences 030302 biochemistry & molecular biology Membrane Proteins Cell Biology N-Acetylneuraminic Acid Microscopy Electron Membrane Microscopy Fluorescence chemistry Membrane protein 570 Life sciences biology Peptides N-Acetylneuraminic acid |
| Zdroj: | Biochimica et Biophysica Acta |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2011.06.007 |
| Popis: | Cationic antimicrobial peptides (CAMPs) selectively target bacterial membranes by electrostatic interactions with negatively charged lipids. It turned out that for inhibition of microbial growth a high CAMP membrane concentration is required, which can be realized by the incorporation of hydrophobic groups within the peptide. Increasing hydrophobicity, however, reduces the CAMP selectivity for bacterial over eukaryotic host membranes, thereby causing the risk of detrimental side-effects. In this study we addressed how cationic amphipathic peptides—in particular a CAMP with Lysine–Leucine–Lysine repeats (termed KLK)—affect the localization and dynamics of molecules in eukaryotic membranes. We found KLK to selectively inhibit the endocytosis of a subgroup of membrane proteins and lipids by electrostatically interacting with negatively charged sialic acid moieties. Ultrastructural characterization revealed the formation of membrane invaginations representing fission or fusion intermediates, in which the sialylated proteins and lipids were immobilized. Experiments on structurally different cationic amphipathic peptides (KLK, 6-MO-LF11-322 and NK14-2) indicated a cooperation of electrostatic and hydrophobic forces that selectively arrest sialylated membrane constituents. Research highlights ► Cationic antimicrobial peptide KLK affects eukaryotic host cells ► KLK induces accumulation of plasma mebrane proteins/lipids ► Dependent on sialic acid residues ► Application of KLK leads to a recycling inhibition of sialyted molecules |
| Databáze: | OpenAIRE |
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