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Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides.
Lázár, Viktória; Martins, Ana; Spohn, Réka; Daruka, Lejla; Grézal, Gábor; Fekete, Gergely; Számel, Mónika; Jangir, Pramod K; Kintses, Bálint; Csörgo, Bálint; Nyerges, Ákos; Györkei, Ádám; Kincses, András; Dér, András; Walter, Fruzsina R; Deli, Mária A; Urbán, Edit; Hegedus, Zsófia; Olajos, Gábor; Méhi, Orsolya; Bálint, Balázs; Nagy, István; Martinek, Tamás A; Papp, Balázs; Pál, Csaba.
Afiliación
  • Lázár V; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Martins A; Faculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel.
  • Spohn R; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Daruka L; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Grézal G; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Fekete G; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Számel M; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Jangir PK; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Kintses B; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Csörgo B; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Nyerges Á; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Györkei Á; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Kincses A; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Dér A; Biomolecular Electronics Research Group, Bionanoscience Unit, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Walter FR; Biomolecular Electronics Research Group, Bionanoscience Unit, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Deli MA; Biological Barriers Research Group, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Urbán E; Biological Barriers Research Group, Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Hegedus Z; Institute of Clinical Microbiology, Albert Szent-Györgyi Medical and Pharmaceutical Center, Faculty of Medicine, University of Szeged, Szeged, Hungary.
  • Olajos G; Institute of Pharmaceutical Analysis, University of Szeged, Szeged, Hungary.
  • Méhi O; Institute of Pharmaceutical Analysis, University of Szeged, Szeged, Hungary.
  • Bálint B; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary.
  • Nagy I; SeqOmics Biotechnology Ltd, Mórahalom, Hungary.
  • Martinek TA; SeqOmics Biotechnology Ltd, Mórahalom, Hungary.
  • Papp B; Sequencing Platform, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Pál C; Institute of Pharmaceutical Analysis, University of Szeged, Szeged, Hungary.
Nat Microbiol ; 3(6): 718-731, 2018 06.
Article en En | MEDLINE | ID: mdl-29795541
Antimicrobial peptides are promising alternative antimicrobial agents. However, little is known about whether resistance to small-molecule antibiotics leads to cross-resistance (decreased sensitivity) or collateral sensitivity (increased sensitivity) to antimicrobial peptides. We systematically addressed this question by studying the susceptibilities of a comprehensive set of 60 antibiotic-resistant Escherichia coli strains towards 24 antimicrobial peptides. Strikingly, antibiotic-resistant bacteria show a high frequency of collateral sensitivity to antimicrobial peptides, whereas cross-resistance is relatively rare. We identify clinically relevant multidrug-resistance mutations that increase bacterial sensitivity to antimicrobial peptides. Collateral sensitivity in multidrug-resistant bacteria arises partly through regulatory changes shaping the lipopolysaccharide composition of the bacterial outer membrane. These advances allow the identification of antimicrobial peptide-antibiotic combinations that enhance antibiotic activity against multidrug-resistant bacteria and slow down de novo evolution of resistance. In particular, when co-administered as an adjuvant, the antimicrobial peptide glycine-leucine-amide caused up to 30-fold decrease in the antibiotic resistance level of resistant bacteria. Our work provides guidelines for the development of efficient peptide-based therapies of antibiotic-resistant infections.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos Catiónicos Antimicrobianos / Farmacorresistencia Bacteriana Múltiple / Escherichia coli / Antibacterianos Tipo de estudio: Diagnostic_studies / Guideline Idioma: En Revista: Nat Microbiol Año: 2018 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos Catiónicos Antimicrobianos / Farmacorresistencia Bacteriana Múltiple / Escherichia coli / Antibacterianos Tipo de estudio: Diagnostic_studies / Guideline Idioma: En Revista: Nat Microbiol Año: 2018 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Reino Unido