%0 Journal Article
%A Di Somma, Angela
%A Avitabile, Concetta
%A Cirillo, Arianna
%A Moretta, Antonio
%A Merlino, Antonello
%A Paduano, Luigi
%A Duilio, Angela
%A Romanelli, Alessandra
%T The antimicrobial peptide Temporin L impairs E. coli cell division by interacting with FtsZ and the divisome complex
%J Biochimica et biophysica acta / General subjects
%V 1864
%N 7
%@ 0304-4165
%C Amsterdam [u.a.]
%I Elsevier
%M FZJ-2020-05396
%P 129606
%D 2020
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 32229224
%U <Go to ISI:>//WOS:000536132200017
%R 10.1016/j.bbagen.2020.129606
%U https://juser.fz-juelich.de/record/889023