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Antimicrobial Peptides from the Aurein Family Form Ion‐Selective Pores in Bacillus subtilis
Author(s) -
Wenzel Michaela,
Senges Christoph Helmut Rudi,
Zhang Jin,
Suleman Selina,
Nguyen Michael,
Kumar Prashant,
Chiriac Alina Iulia,
Stepanek Jennifer Janina,
Raatschen Nadja,
May Caroline,
Krämer Ute,
Sahl HansGeorg,
Straus Suzana Katarina,
Bandow Julia Elisabeth
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500020
Subject(s) - bacillus subtilis , chemistry , antimicrobial peptides , propidium iodide , biophysics , cell envelope , intracellular , membrane , biochemistry , cell membrane , metal ions in aqueous solution , peptide , bacteria , metal , biology , escherichia coli , organic chemistry , apoptosis , genetics , programmed cell death , gene
The mechanism of action of aurein 2.2 and aurein 2.3, antimicrobial peptides from the frog Litoria aurea , was investigated. Proteomic profiling of the Bacillus subtilis stress response indicates that the cell envelope is the main target for both aureins. Upon treatment, the cytoplasmic membrane depolarizes and cellular ATP levels decrease. Global element analysis shows that intracellular concentrations of certain metal ions (potassium, magnesium, iron, and manganese) strongly decrease. Selective translocation of some ions over others was demonstrated in vitro. The same set of ions also leaks from B. subtilis cells treated with sublethal concentrations of gramicidin S, MP196, and nisin. Aureins do not permeabilize the cell membrane for propidium iodide thus excluding formation of large, unspecific pores. Our data suggest that the aureins acts by forming small pores thereby causing membrane depolarization, and by triggering the release of certain metal ions thus disturbing cellular ion homeostasis.