Studies on the interactions of neutral Galleria mellonella cecropin D with living bacterial cells

Amino Acids
Agnieszka Zdybicka-BarabasMałgorzata Cytryńska

Abstract

Cecropins constitute an important family of insect antimicrobial peptides involved in humoral innate immune response. In comparison with the highly basic cecropins A and B, cecropins D are less cationic and more hydrophobic. Interestingly, cecropins D were described only in lepidopteran insects, e.g., the greater wax moth Galleria mellonella. In the present study, interactions of neutral cecropin D (pI 6.47) purified from hemolymph of G. mellonella with living Escherichia coli cells were investigated. Fluorescence lifetime imaging microscopy using fluorescein isothiocyanate-labeled cecropin D revealed very fast binding of the peptide to E. coli cells. Fourier transform infrared spectroscopy analyses showed that G. mellonella cecropin D interacted especially with E. coli LPS and probably other lipid components of the bacterial cell envelope and exhibited an ordering effect with regard to lipid chains. This effect is consistent with the peptide binding mechanism based upon its incorporation into the lipid phase of the cell membrane. The interaction resulted in permeabilization of the bacterial cell membrane. Upon cecropin D binding, the cells lost characteristic surface topography, which was accompanied by altered nanomechanical ...Continue Reading

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Citations

Jul 1, 2020·European Journal of Pharmacology·Maksymilian ZiajaAgnieszka Piastowska-Ciesielska
Feb 27, 2021·Frontiers in Cellular and Infection Microbiology·Masanori AsaiSandra M Newton
Aug 25, 2020·Biochimica Et Biophysica Acta. Biomembranes·Katharine HammondBart W Hoogenboom

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Methods Mentioned

BETA
fluorescence lifetime
atomic
transmission electron microscopy
electrophoresis
gel filtration
AFM
force measurements
fluorescence
fluorescence microscopy
circular dichroism

Software Mentioned

ThermoGalactic
NanoScope
Jpred4
Grams Al
SymPhoTime

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