The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.

The rhizosphere isolate Pseudomonas putida BW11M1 produces a mixture of cyclic lipopeptide congeners, designated xantholysins. Properties of the major compound xantholysin A, shared with several other Pseudomonas lipopeptides, include antifungal activity and toxicity to Gram-positive bacteria, a sup...

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Autores principales:	Wen Li, Hassan Rokni-Zadeh, Matthias De Vleeschouwer, Maarten G K Ghequire, Davy Sinnaeve, Guan-Lin Xie, Jef Rozenski, Annemieke Madder, José C Martins, René De Mot
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6bbc7635068d41a3b45e3bd7b077a846
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spelling	oai:doaj.org-article:6bbc7635068d41a3b45e3bd7b077a8462021-11-18T07:45:22ZThe antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.1932-620310.1371/journal.pone.0062946https://doaj.org/article/6bbc7635068d41a3b45e3bd7b077a8462013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23690965/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The rhizosphere isolate Pseudomonas putida BW11M1 produces a mixture of cyclic lipopeptide congeners, designated xantholysins. Properties of the major compound xantholysin A, shared with several other Pseudomonas lipopeptides, include antifungal activity and toxicity to Gram-positive bacteria, a supportive role in biofilm formation, and facilitation of surface colonization through swarming. Atypical is the lipopeptide's capacity to inhibit some Gram-negative bacteria, including several xanthomonads. The lipotetradecadepsipeptides are assembled by XtlA, XtlB and XtlC, three co-linearly operating non-ribosomal peptide synthetases (NRPSs) displaying similarity in modular architecture with the entolysin-producing enzymes of the entomopathogenic Pseudomonas entomophila L48. A shifted serine-incorporating unit in the eight-module enzyme XtlB elongating the central peptide moiety not only generates an amino acid sequence differing at several equivalent positions from entolysin, but also directs xantholysin's macrocyclization into an octacyclic structure, distinct from the pentacyclic closure in entolysin. Relaxed fatty acid specificity during lipoinitiation by XtlA (acylation with 3-hydroxydodec-5-enoate instead of 3-hydroxydecanoate) and for incorporation of the ultimate amino acid by XtlC (valine instead of isoleucine) account for the production of the minor structural variants xantholysin C and B, respectively. Remarkably, the genetic backbones of the xantholysin and entolysin NRPS systems also bear pronounced phylogenetic similarity to those of the P. putida strains PCL1445 and RW10S2, albeit generating the seemingly structurally unrelated cyclic lipopeptides putisolvin (undecapeptide containing a cyclotetrapeptide) and WLIP (nonapeptide containing a cycloheptapeptide), respectively. This similarity includes the linked genes encoding the cognate LuxR-family regulator and tripartite export system components in addition to individual modules of the NRPS enzymes, and probably reflects a common evolutionary origin. Phylogenetic scrutiny of the modules used for selective amino acid activation by these synthetases indicates that bacteria such as pseudomonads recruit and reshuffle individual biosynthetic units and blocks thereof to engineer reorganized or novel NRPS assembly lines for diversified synthesis of lipopeptides.Wen LiHassan Rokni-ZadehMatthias De VleeschouwerMaarten G K GhequireDavy SinnaeveGuan-Lin XieJef RozenskiAnnemieke MadderJosé C MartinsRené De MotPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e62946 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wen Li Hassan Rokni-Zadeh Matthias De Vleeschouwer Maarten G K Ghequire Davy Sinnaeve Guan-Lin Xie Jef Rozenski Annemieke Madder José C Martins René De Mot The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.
description	The rhizosphere isolate Pseudomonas putida BW11M1 produces a mixture of cyclic lipopeptide congeners, designated xantholysins. Properties of the major compound xantholysin A, shared with several other Pseudomonas lipopeptides, include antifungal activity and toxicity to Gram-positive bacteria, a supportive role in biofilm formation, and facilitation of surface colonization through swarming. Atypical is the lipopeptide's capacity to inhibit some Gram-negative bacteria, including several xanthomonads. The lipotetradecadepsipeptides are assembled by XtlA, XtlB and XtlC, three co-linearly operating non-ribosomal peptide synthetases (NRPSs) displaying similarity in modular architecture with the entolysin-producing enzymes of the entomopathogenic Pseudomonas entomophila L48. A shifted serine-incorporating unit in the eight-module enzyme XtlB elongating the central peptide moiety not only generates an amino acid sequence differing at several equivalent positions from entolysin, but also directs xantholysin's macrocyclization into an octacyclic structure, distinct from the pentacyclic closure in entolysin. Relaxed fatty acid specificity during lipoinitiation by XtlA (acylation with 3-hydroxydodec-5-enoate instead of 3-hydroxydecanoate) and for incorporation of the ultimate amino acid by XtlC (valine instead of isoleucine) account for the production of the minor structural variants xantholysin C and B, respectively. Remarkably, the genetic backbones of the xantholysin and entolysin NRPS systems also bear pronounced phylogenetic similarity to those of the P. putida strains PCL1445 and RW10S2, albeit generating the seemingly structurally unrelated cyclic lipopeptides putisolvin (undecapeptide containing a cyclotetrapeptide) and WLIP (nonapeptide containing a cycloheptapeptide), respectively. This similarity includes the linked genes encoding the cognate LuxR-family regulator and tripartite export system components in addition to individual modules of the NRPS enzymes, and probably reflects a common evolutionary origin. Phylogenetic scrutiny of the modules used for selective amino acid activation by these synthetases indicates that bacteria such as pseudomonads recruit and reshuffle individual biosynthetic units and blocks thereof to engineer reorganized or novel NRPS assembly lines for diversified synthesis of lipopeptides.
format	article
author	Wen Li Hassan Rokni-Zadeh Matthias De Vleeschouwer Maarten G K Ghequire Davy Sinnaeve Guan-Lin Xie Jef Rozenski Annemieke Madder José C Martins René De Mot
author_facet	Wen Li Hassan Rokni-Zadeh Matthias De Vleeschouwer Maarten G K Ghequire Davy Sinnaeve Guan-Lin Xie Jef Rozenski Annemieke Madder José C Martins René De Mot
author_sort	Wen Li
title	The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.
title_short	The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.
title_full	The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.
title_fullStr	The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.
title_full_unstemmed	The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.
title_sort	antimicrobial compound xantholysin defines a new group of pseudomonas cyclic lipopeptides.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/6bbc7635068d41a3b45e3bd7b077a846
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The antimicrobial compound xantholysin defines a new group of Pseudomonas cyclic lipopeptides.

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