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  Microbial cationic peptides as a natural defense mechanism against insect antimicrobial peptides

Vo, T. D., Spahn, C., Heilemann, M., & Bode, H. B. (2021). Microbial cationic peptides as a natural defense mechanism against insect antimicrobial peptides. ACS Chemical Biology, 16(3), 447-451. doi:10.1021/acschembio.0c00794.

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https://doi.org/10.1021/acschembio.0c00794 (Verlagsversion)
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 Urheber:
Vo, Tien Duy1, Autor
Spahn, Christoph2, Autor
Heilemann, Mike2, Autor
Bode, Helge B.1, Autor           
Affiliations:
1Natural Product Function and Engineering, Department of Natural Products in Organismic Interactions, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Karl-von-Frisch-Strasse 10, D-35043 Marburg, DE, ou_3266308              
2external, ou_persistent22              

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 Zusammenfassung: Bacteria produce a plethora of specialized metabolites (SM), with the
ecological function of most of them not known. A major group of SM are
peptides derived from nonribosomal peptide synthetases (NRPS). In
entomopathogenic bacteria of the genus Xenorhabdus, PAX
(peptide-antimicrobial-Xenorhabdus) were described as NRPS-derived
lipopeptides, which show antimicrobial activities against bacteria and
fungi. We analyzed the production of PAX in Xenorhabdus doucetiae and
found the majority bound to the cells. We derivatized PAX with
fluorophores and show binding to cells when added externally using
super-resolution microscopy. Externally added PAX in X. doucetiae and E.
coli as well as inducible PAX production in X. doucetiae showed a
protective effect against various antimicrobial peptides (AMPs) from
insects, where they are used as a defense mechanism against pathogens.
Because AMPs are often positively charged, our results suggest a
PAX-induced repulsive force due to positive charge at the bacterial cell
wall.

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Sprache(n): eng - English
 Datum: 2021-02-17
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000631431900001
DOI: 10.1021/acschembio.0c00794
 Art des Abschluß: -

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Titel: ACS Chemical Biology
  Kurztitel : ACS Chem. Biol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 16 (3) Artikelnummer: - Start- / Endseite: 447 - 451 Identifikator: ISSN: 1554-8929
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000035040