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Initial Characterization of the Viridisins' Biological Properties.
Vermeulen, Ross Rayne; van Staden, Anton Du Preez; Ollewagen, Tracey; van Zyl, Leonardo Joaquim; Luo, Youran; van der Donk, Wilfred A; Dicks, Leon Milner Theodore; Smith, Carine; Trindade, Marla.
Afiliación
  • Vermeulen RR; Department of Microbiology, Stellenbosch University, Matieland 7602, South Africa.
  • van Staden ADP; Institute for Microbial Biotechnology and Metagenomics, University of the Western Cape, Level 2 New Life Sciences Building, Robert Sobukwe Rd, Bellville 7535, South Africa.
  • Ollewagen T; Experimental Research Group, Faculty of Medicine and Health Sciences, Department of Medicine, Stellenbosch University, Francie van Zijl Drive, Parow 7499, South Africa.
  • van Zyl LJ; Experimental Research Group, Faculty of Medicine and Health Sciences, Department of Medicine, Stellenbosch University, Francie van Zijl Drive, Parow 7499, South Africa.
  • Luo Y; Institute for Microbial Biotechnology and Metagenomics, University of the Western Cape, Level 2 New Life Sciences Building, Robert Sobukwe Rd, Bellville 7535, South Africa.
  • van der Donk WA; Department of Chemistry and Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
  • Dicks LMT; Department of Chemistry and Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
  • Smith C; Department of Microbiology, Stellenbosch University, Matieland 7602, South Africa.
  • Trindade M; Experimental Research Group, Faculty of Medicine and Health Sciences, Department of Medicine, Stellenbosch University, Francie van Zijl Drive, Parow 7499, South Africa.
ACS Omega ; 9(29): 31832-31841, 2024 Jul 23.
Article en En | MEDLINE | ID: mdl-39072090
ABSTRACT
Viridisin A1 and A2 were previously heterologously expressed, purified, and characterized as ribosomally produced and post-translationally modified lanthipeptides. Such lanthipeptide operons are surprisingly common in Gram-negative bacteria, although their expression seems to be predominantly cryptic under laboratory conditions. However, the bioactivity and biological role of most lanthipeptide operons originating from marine-associated Pseudomonadota, such asThalassomonas viridans XOM25T, have not been described. Therefore, marine-associated Gram-negative lanthipeptide operons represent an untapped resource for novel structures, biochemistries, and bioactivities. Here, the upscaled production of viridisin A1 and A2 was performed for (methyl)lanthionine stereochemistry characterization, antibacterial, antifungal, and larval zebrafish behavioral screening. While antimicrobial activity was not observed, the VirBC modification machinery was found to install both dl- and ll-lanthionine stereoisomers. The VdsA1 and VdsA2 peptides induced sedative and stimulatory effects in zebrafish larvae, respectively, which is a bioactivity not previously reported from lanthipeptides. When combined, VdsA1 and VdsA2 counteracted the sedative and stimulatory effects observed when used individually.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: ACS Omega Año: 2024 Tipo del documento: Article País de afiliación: Sudáfrica Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: ACS Omega Año: 2024 Tipo del documento: Article País de afiliación: Sudáfrica Pais de publicación: Estados Unidos