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. 2020 Jul;1864(7):129606.
doi: 10.1016/j.bbagen.2020.129606. Epub 2020 Mar 27.

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

Angela Di Somma  1 , Concetta Avitabile  2 , Arianna Cirillo  3 , Antonio Moretta  4 , Antonello Merlino  3 , Luigi Paduano  3 , Angela Duilio  5 , Alessandra Romanelli  6
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Free article

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

Angela Di Somma et al. Biochim Biophys Acta Gen Subj. 2020 Jul.
Free article

Abstract

Background: The 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.

Methods: In 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.

Results: We 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.

Conclusions: The peptide temporin L acts by a non-membrane-lytic mechanism of action, inhibiting the divisome machinery.

General significance: Identification of _targets of antimicrobial peptides is pivotal to the tailored design of new antimicrobials.

Keywords: Antimicrobial; Cell division; FtsZ; Inhibitor; Peptide; Proteomics; Small angle neutron scattering; Temporin L.

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Conflict of interest statement

Declaration of Competing Interest The authors declare that they have no conflicts of interest with the contents of this article.

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