TY - JOUR
AU - Di Somma, Angela
AU - Avitabile, Concetta
AU - Cirillo, Arianna
AU - Moretta, Antonio
AU - Merlino, Antonello
AU - Paduano, Luigi
AU - Duilio, Angela
AU - Romanelli, Alessandra
TI - The antimicrobial peptide Temporin L impairs E. coli cell division by interacting with FtsZ and the divisome complex
JO - Biochimica et biophysica acta / General subjects
VL - 1864
IS - 7
SN - 0304-4165
CY - Amsterdam [u.a.]
PB - Elsevier
M1 - FZJ-2020-05396
SP - 129606
PY - 2020
AB - 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.
LB - PUB:(DE-HGF)16
C6 - 32229224
UR - <Go to ISI:>//WOS:000536132200017
DO - DOI:10.1016/j.bbagen.2020.129606
UR - https://juser.fz-juelich.de/record/889023
ER -