The antimicrobial peptide Temporin L impairs E. coli cell division by interacting with FtsZ and the divisome complex.
Biochim Biophys Acta Gen Subj
; 1864(7): 129606, 2020 07.
Article
in En
| MEDLINE
| ID: mdl-32229224
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. GENERALSIGNIFICANCE:
Identification of targets of antimicrobial peptides is pivotal to the tailored design of new antimicrobials.Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Escherichia coli
/
Antimicrobial Peptides
Language:
En
Journal:
Biochim Biophys Acta Gen Subj
Year:
2020
Document type:
Article
Affiliation country:
Italy