Standard

Natural antimicrobial peptide complexes in the fighting of antibiotic resistant biofilms : Calliphora vicina medicinal maggots. / Gordya, Natalia; Yakovlev, Andrey; Kruglikova, Anastasia; Tulin, Dmitry; Potolitsina, Evdokia; Suborova, Tatyana; Bordo, Domenico; Rosano, Camillo; Chernysh, Sergey.

в: PLoS ONE, Том 12, № 3, e0173559, 03.2017.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

APA

Vancouver

Author

Gordya, Natalia ; Yakovlev, Andrey ; Kruglikova, Anastasia ; Tulin, Dmitry ; Potolitsina, Evdokia ; Suborova, Tatyana ; Bordo, Domenico ; Rosano, Camillo ; Chernysh, Sergey. / Natural antimicrobial peptide complexes in the fighting of antibiotic resistant biofilms : Calliphora vicina medicinal maggots. в: PLoS ONE. 2017 ; Том 12, № 3.

BibTeX

@article{6957cc6658064e949a6ed5112359c9e8,
title = "Natural antimicrobial peptide complexes in the fighting of antibiotic resistant biofilms: Calliphora vicina medicinal maggots",
abstract = "Biofilms, sedimented microbial communities embedded in a biopolymer matrix cause vast majority of human bacterial infections and many severe complications such as chronic inflammatory diseases and cancer. Biofilms' resistance to the host immunity and antibiotics makes this kind of infection particularly intractable. Antimicrobial peptides (AMPs) are a ubiquitous facet of innate immunity in animals. However, AMPs activity was studied mainly on planktonic bacteria and little is known about their effects on biofilms. We studied structure and anti-biofilm activity of AMP complex produced by the maggots of blowfly Calliphora vicina living in environments extremely contaminated by biofilm-forming germs. The complex exhibits strong cell killing and matrix destroying activity against human pathogenic antibiotic resistant Escherichia coli, Staphylococcus aureus and Acinetobacter baumannii biofilms as well as non-Toxicity to human immune cells. The complex was found to contain AMPs from defensin, cecropin, diptericin and proline-rich peptide families simultaneously expressed in response to bacterial infection and encoded by hundreds mRNA isoforms. All the families combine cell killing and matrix destruction mechanisms, but the ratio of these effects and antibacterial activity spectrum are specific to each family. These molecules dramatically extend the list of known anti-biofilm AMPs. However, pharmacological development of the complex as a whole can provide significant advantages compared with a conventional onecomponent approach. In particular, a similar level of activity against biofilm and planktonic bacteria (MBEC/MIC ratio) provides the complex advantage over conventional antibiotics. Available methods of the complex in situ and in vitro biosynthesis make this idea practicable.",
author = "Natalia Gordya and Andrey Yakovlev and Anastasia Kruglikova and Dmitry Tulin and Evdokia Potolitsina and Tatyana Suborova and Domenico Bordo and Camillo Rosano and Sergey Chernysh",
note = "Publisher Copyright: {\textcopyright} 2017 Gordya et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",
year = "2017",
month = mar,
doi = "10.1371/journal.pone.0173559",
language = "English",
volume = "12",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "3",

}

RIS

TY - JOUR

T1 - Natural antimicrobial peptide complexes in the fighting of antibiotic resistant biofilms

T2 - Calliphora vicina medicinal maggots

AU - Gordya, Natalia

AU - Yakovlev, Andrey

AU - Kruglikova, Anastasia

AU - Tulin, Dmitry

AU - Potolitsina, Evdokia

AU - Suborova, Tatyana

AU - Bordo, Domenico

AU - Rosano, Camillo

AU - Chernysh, Sergey

N1 - Publisher Copyright: © 2017 Gordya et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2017/3

Y1 - 2017/3

N2 - Biofilms, sedimented microbial communities embedded in a biopolymer matrix cause vast majority of human bacterial infections and many severe complications such as chronic inflammatory diseases and cancer. Biofilms' resistance to the host immunity and antibiotics makes this kind of infection particularly intractable. Antimicrobial peptides (AMPs) are a ubiquitous facet of innate immunity in animals. However, AMPs activity was studied mainly on planktonic bacteria and little is known about their effects on biofilms. We studied structure and anti-biofilm activity of AMP complex produced by the maggots of blowfly Calliphora vicina living in environments extremely contaminated by biofilm-forming germs. The complex exhibits strong cell killing and matrix destroying activity against human pathogenic antibiotic resistant Escherichia coli, Staphylococcus aureus and Acinetobacter baumannii biofilms as well as non-Toxicity to human immune cells. The complex was found to contain AMPs from defensin, cecropin, diptericin and proline-rich peptide families simultaneously expressed in response to bacterial infection and encoded by hundreds mRNA isoforms. All the families combine cell killing and matrix destruction mechanisms, but the ratio of these effects and antibacterial activity spectrum are specific to each family. These molecules dramatically extend the list of known anti-biofilm AMPs. However, pharmacological development of the complex as a whole can provide significant advantages compared with a conventional onecomponent approach. In particular, a similar level of activity against biofilm and planktonic bacteria (MBEC/MIC ratio) provides the complex advantage over conventional antibiotics. Available methods of the complex in situ and in vitro biosynthesis make this idea practicable.

AB - Biofilms, sedimented microbial communities embedded in a biopolymer matrix cause vast majority of human bacterial infections and many severe complications such as chronic inflammatory diseases and cancer. Biofilms' resistance to the host immunity and antibiotics makes this kind of infection particularly intractable. Antimicrobial peptides (AMPs) are a ubiquitous facet of innate immunity in animals. However, AMPs activity was studied mainly on planktonic bacteria and little is known about their effects on biofilms. We studied structure and anti-biofilm activity of AMP complex produced by the maggots of blowfly Calliphora vicina living in environments extremely contaminated by biofilm-forming germs. The complex exhibits strong cell killing and matrix destroying activity against human pathogenic antibiotic resistant Escherichia coli, Staphylococcus aureus and Acinetobacter baumannii biofilms as well as non-Toxicity to human immune cells. The complex was found to contain AMPs from defensin, cecropin, diptericin and proline-rich peptide families simultaneously expressed in response to bacterial infection and encoded by hundreds mRNA isoforms. All the families combine cell killing and matrix destruction mechanisms, but the ratio of these effects and antibacterial activity spectrum are specific to each family. These molecules dramatically extend the list of known anti-biofilm AMPs. However, pharmacological development of the complex as a whole can provide significant advantages compared with a conventional onecomponent approach. In particular, a similar level of activity against biofilm and planktonic bacteria (MBEC/MIC ratio) provides the complex advantage over conventional antibiotics. Available methods of the complex in situ and in vitro biosynthesis make this idea practicable.

UR - http://www.scopus.com/inward/record.url?scp=85014840762&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0173559

DO - 10.1371/journal.pone.0173559

M3 - Article

C2 - 28278280

AN - SCOPUS:85014840762

VL - 12

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 3

M1 - e0173559

ER -

ID: 14086386