Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes

Eukaryotic antimicrobial peptides (AMPs) interact with plasma membrane of bacteria, fungi and eukaryotic parasites. Noteworthy, Lactobacillus delbrueckii subsp. lactis (CIDCA 133) and L. delbrueckii subsp. bulgaricus (CIDCA 331) show different susceptibility to human beta-defensins (β-sheet peptides...

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Detalles Bibliográficos
Publicado: 2019
Materias:
Aurein
Citropin
Lactobacilli
Maculatin
α helix antimicrobial peptides
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1861_n6_p1069_Szymanowski
http://hdl.handle.net/20.500.12110/paper_00052736_v1861_n6_p1069_Szymanowski
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_00052736_v1861_n6_p1069_Szymanowski
record_format dspace
spelling paper:paper_00052736_v1861_n6_p1069_Szymanowski2023-06-08T14:29:52Z Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes Aurein Citropin Lactobacilli Maculatin α helix antimicrobial peptides Eukaryotic antimicrobial peptides (AMPs) interact with plasma membrane of bacteria, fungi and eukaryotic parasites. Noteworthy, Lactobacillus delbrueckii subsp. lactis (CIDCA 133) and L. delbrueckii subsp. bulgaricus (CIDCA 331) show different susceptibility to human beta-defensins (β-sheet peptides). In the present work we extended the study to α-helical peptides from anuran amphibian (Aurein 1.2, Citropin 1.1 and Maculatin 1.1). We studied the effect on whole bacteria and liposomes formulated with bacterial lipids through growth kinetics, flow cytometry, leakage of liposome content and studies of peptide insertion in lipid monolayers. Growth of strain CIDCA 331 was dramatically inhibited in the presence of all three peptides and minimal inhibitory concentrations were lower than those for strain CIDCA 133. Flow cytometry revealed that AMPs lead to the permeabilization of bacteria. In addition, CIDCA 331-derived liposomes showed high susceptibility, leading to content leakage and structural disruption. Accordingly, peptide insertion in lipid monolayers demonstrated spontaneous interaction of AMPs with CIDCA 331 lipids. In contrast, lipids monolayers from strain CIDCA 133 were less susceptible. Summarizing we demonstrate that the high resistance of the probiotic strain CIDCA 133 to AMPs extends to α helix peptides Aurein, Citropin and Maculatin. This behavior could be ascribed in part to differences in membrane composition. These findings, along with the previously demonstrated resistance to β defensins from human origin, suggest that strain CIDCA 133 is well adapted to host innate immune effectors from both mammals and amphibians thus indicating conserved mechanisms of interaction with key components of the innate immune system. © 2019 Elsevier B.V. 2019 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1861_n6_p1069_Szymanowski http://hdl.handle.net/20.500.12110/paper_00052736_v1861_n6_p1069_Szymanowski
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Aurein
Citropin
Lactobacilli
Maculatin
α helix antimicrobial peptides
spellingShingle Aurein
Citropin
Lactobacilli
Maculatin
α helix antimicrobial peptides
Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
topic_facet Aurein
Citropin
Lactobacilli
Maculatin
α helix antimicrobial peptides
description Eukaryotic antimicrobial peptides (AMPs) interact with plasma membrane of bacteria, fungi and eukaryotic parasites. Noteworthy, Lactobacillus delbrueckii subsp. lactis (CIDCA 133) and L. delbrueckii subsp. bulgaricus (CIDCA 331) show different susceptibility to human beta-defensins (β-sheet peptides). In the present work we extended the study to α-helical peptides from anuran amphibian (Aurein 1.2, Citropin 1.1 and Maculatin 1.1). We studied the effect on whole bacteria and liposomes formulated with bacterial lipids through growth kinetics, flow cytometry, leakage of liposome content and studies of peptide insertion in lipid monolayers. Growth of strain CIDCA 331 was dramatically inhibited in the presence of all three peptides and minimal inhibitory concentrations were lower than those for strain CIDCA 133. Flow cytometry revealed that AMPs lead to the permeabilization of bacteria. In addition, CIDCA 331-derived liposomes showed high susceptibility, leading to content leakage and structural disruption. Accordingly, peptide insertion in lipid monolayers demonstrated spontaneous interaction of AMPs with CIDCA 331 lipids. In contrast, lipids monolayers from strain CIDCA 133 were less susceptible. Summarizing we demonstrate that the high resistance of the probiotic strain CIDCA 133 to AMPs extends to α helix peptides Aurein, Citropin and Maculatin. This behavior could be ascribed in part to differences in membrane composition. These findings, along with the previously demonstrated resistance to β defensins from human origin, suggest that strain CIDCA 133 is well adapted to host innate immune effectors from both mammals and amphibians thus indicating conserved mechanisms of interaction with key components of the innate immune system. © 2019 Elsevier B.V.
title Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
title_short Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
title_full Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
title_fullStr Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
title_full_unstemmed Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
title_sort differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
publishDate 2019
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1861_n6_p1069_Szymanowski
http://hdl.handle.net/20.500.12110/paper_00052736_v1861_n6_p1069_Szymanowski
_version_ 1768544483719249920

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