Journal Article FZJ-2020-05396

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The antimicrobial peptide Temporin L impairs E. coli cell division by interacting with FtsZ and the divisome complex

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2020
Elsevier Amsterdam [u.a.]

Biochimica et biophysica acta / General subjects 1864(7), 129606 () [10.1016/j.bbagen.2020.129606]

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Abstract: BackgroundThe comprehension of the mechanism of action of antimicrobial peptides is fundamental for the design of new antibiotics. Studies performed looking at the interaction of peptides with bacterial cells offer a faithful picture of what really happens in nature.MethodsIn this work we focused on the interaction of the peptide Temporin L with E. coli cells, using a variety of biochemical and biophysical techniques that include: functional proteomics, docking, optical microscopy, TEM, DLS, SANS, fluorescence.ResultsWe identified bacterial proteins specifically interacting with the peptides that belong to the divisome machinery; our data suggest that the GTPase FtsZ is the specific peptide target. Docking experiments supported the FtsZ-TL interaction; binding and enzymatic assays using recombinant FtsZ confirmed this hypothesis and revealed a competitive inhibition mechanism. Optical microscopy and TEM measurements demonstrated that, upon incubation with the peptide, bacterial cells are unable to divide forming long necklace-like cell filaments. Dynamic light scattering studies and Small Angle Neutron Scattering experiments performed on treated and untreated bacterial cells, indicated a change at the nanoscale level of the bacterial membrane.ConclusionsThe peptide temporin L acts by a non-membrane-lytic mechanism of action, inhibiting the divisome machinery.

Keyword(s): Health and Life (1st) ; Biology (2nd) ; Soft Condensed Matter (2nd)

Classification:

Contributing Institute(s):
  1. JCNS-FRM-II (JCNS-FRM-II)
  2. Heinz Maier-Leibnitz Zentrum (MLZ)
Research Program(s):
  1. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)
  2. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
Experiment(s):
  1. KWS-2: Small angle scattering diffractometer (NL3ao)
  2. KWS-3: Very small angle scattering diffractometer with focusing mirror (NL3auS)

Appears in the scientific report 2020
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Medline ; Creative Commons Attribution-NonCommercial-NoDerivs CC BY-NC-ND 4.0 ; Embargoed OpenAccess ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2020-12-22, last modified 2021-04-01


Published on 2020-03-27. Available in OpenAccess from 2021-03-27.:
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