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
em En
| MEDLINE
| ID: mdl-32229224
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.
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MEDLINE
Assunto principal:
Escherichia coli
/
Peptídeos Antimicrobianos
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article