Serratamolide, a Metabolic Product of Serratia

Wasserman, Harry H.; Keggi, Janis J.; McKeon, James E.

doi:10.1021/ja01480a046

Cited by 78 publications

(39 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…serratamolide reported previously as an antibiotic (22,23). It is interesting that production of these serrawettins is also temperature-dependent (10).…”

mentioning

confidence: 75%

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Sunaga

Sato

et al. 2004

Microbiology and Immunology

View full text Add to dashboard Cite

Serratia marcescens mutants defective in production of the red pigment prodigiosin and the biosurfactant serrawettin W1 in parallel were isolated by transposon mutagenesis of strain 274. Cloning of the DNA fragment required for production of these secondary metabolites with different chemical structures pointed out a novel open reading frame (ORF) named pswP. The putative product PswP (230 aa) has the distinct signature sequence consensus among members of phosphopantetheinyl transferase (PPTase) which phosphopantetheinylates peptidyl carrier protein (PCP) mostly integrated in the nonribosomal peptide synthetases (NRPSs) system. Since serrawettin W1 belongs to the cyclodepsipeptides, which are biosynthesized through the NRPSs system, and one pyrrole ring in prodigiosin has been reported as a derivative of L‐proline tethered to phosphopantetheinylated PCP, the mutation in the single gene pswP seems responsible for parallel failure in production of prodigiosin and serrawettin W1.

show abstract

“…serratamolide reported previously as an antibiotic (22,23). It is interesting that production of these serrawettins is also temperature-dependent (10).…”

mentioning

confidence: 75%

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Sunaga

Sato

et al. 2004

Microbiology and Immunology

View full text Add to dashboard Cite

show abstract

“…Serrawettin W1, produced by many pigmented S. marcescens strains, is a surface-active cyclodepsipeptide [cyclo-(D-3-hydroxydecanoyl-L-seryl) 2 ] identical to serratamolide, which was discovered by Wasserman et al as an antibiotic (23,24). Serrawettin gets its name by virtue of its wetting activity on various hydrophobic and hydrophilic surfaces (14).…”

Section: Discussionmentioning

confidence: 99%

Mutational analysis of flagellum-independent surface spreading of Serratia marcescens 274 on a low-agar medium

1995

View full text Add to dashboard Cite

In a previous study (J. O'Rear, L. Alberti, and R. M. Harshey, J. Bacteriol. 174:6125-6137, 1992) we reported the isolation of several transposon mutants of Serratia marcescens 274 that were defective either in swarming alone or in both swimming and swarming motility. All the nonflagellate (Fla ؊ ) mutants, while defective in both types of motility, were able to spread rapidly on the surface of low-agar (0.35%) media. We show here that some of the swarming-defective mutants are defective in the production of serrawettin W1, an extracellular cyclic lipopeptide produced by S. marcescens 274. When combined with a Fla defect, the serrawettin (Swt) mutants are deficient in spreading on low-agar media. The spreading deficiency can be overcome by serrawettin supplied extracellularly. Introduction of Fla defects into chemotaxis mutants does not affect this mode of surface translocation. These results suggest that spreading may be a passive form of translocation. We also report that swarming defects in all mutants showing a Dps phenotype (able to swarm within the inoculated area but unable to move outward) in the earlier study can be overcome by changing the commercial source of agar.Serratia marcescens is a pigmented enteric bacterium found in variety of niches, which include soil, water, air, plants, and animals (9). It is also an opportunistic human pathogen, causing many nosocomial infections (7). S. marcescens is unique among enteric bacteria in many respects. It secretes extracellular chitinases, several proteases, a nuclease, and a lipase (13) and produces a wetting agent or surfactant called serrawettin, which helps in the colonization of surfaces (14,15,17). In keeping with its varied habitat, S. marcescens produces alternate forms of differentially flagellated cells which display different types of motility depending on whether the growth medium is liquid or solid (2). Nonflagellated cells of S. marcescens can also translocate (spread) efficiently over the surface of low-agar media (20).Surface colonization via swarming requires the flagellar apparatus as well the chemotaxis system (20). A large-scale transposon mutagenesis study of S. marcescens identified several additional functions that were needed for swarming (20). A sizable subset of the mutants showed a Dps phenotype (cells were capable of swarming but remained confined to the inoculated area, i.e., were unable to move outwards). A distinct group of the Dps mutants (DpsI) appeared not to produce the extracellular slime layer generally visible around the bacterial colony. We show here that some of the DpsI mutants as well as some Dis (completely defective in swarming) mutants are defective in the production of serrawettin W1, an extracellular cyclic lipopeptide (14, 24). Flagellum-independent spreading of S. marcescens 274 on the surface of low-agar media also requires serrawettin. Defects in chemotaxis functions, however, had no effect on this mode of surface colonization. Our results reveal the importance of bacterial surface layers (serrawettins, slim...

show abstract

“…The extracellular products responsible for such activity were isolated and named serrawettins (lipopeptides produced by S. marcescens) (15,16) and rubiwettins [,-D-glucopyranosyl 3-(3'-hydroxytetradecanoyloxy)decanoate and its glucosefree relatives produced by S. rubidaea] (13). Serrawettin Wi, produced by many pigmented S. marcescens strains, is a surface-active cyclodepsipeptide identical to serratamolide, which was discovered by Wasserman as an antibiotic (25,26). Serrawettins W2 and W3 are also surface-active exolipids of nonpigmented strains of S. marcescens (W2 from strain NS 25 and W3 from strains NS 45 and NS 50).…”

mentioning

confidence: 99%

A novel extracellular cyclic lipopeptide which promotes flagellum-dependent and -independent spreading growth of Serratia marcescens

et al. 1992

View full text Add to dashboard Cite

Serrawettin W2, a surface-active exolipid produced by nonpigmented Serratia marcescens NS 25, was examined for its chemical structure and physiological functions. The chemical structure was determined by degradation analyses, infrared spectroscopy, mass spectrometry, and proton magnetic resonance spectroscopy.Serrawettin W2 was shown to be a novel cyclodepsipeptide containing a fatty acid (3-hydroxydecanoic acid) and five amino acids. The peptide was proposed to be D-leucine (N-bonded to the carboxylate of the fatty acid)-L-serine-L-threonine-D-phenylalanine-L-isoleucine (bonded to the 3-hydroxyl group). By examining the effects of isolated serrawettin W2 on serrawettinless mutants, this lipopeptide was shown to be active in the promotion of flagellum-independent spreading growth of the bacteria on a hard agar surface. The parent strain NS 25 formed a giant colony with a self-similar characteristic after incubation for a relatively long time (1 to 2 weeks), similar to other fractal colony-producing strains of S. marcescens (producers of the different serrawettins Wl and W3). On a semisolid medium that permitted flagellum-dependent spreading growth, an external supply of serrawettin W2 accelerated surface translocation of a serrawettinless mutant during a short period (12 h) of observation. In contrast, bacterial translocation in the subsurface space of the semisolid agar was not enhanced by serrawettins. Thus, the extracellular lipids seem to contribute specifically to the surface translocation of the bacteria by exhibiting surfactant activity.Previously, we reported that Serratia marcescens and Serratia rubidaea demonstrate wetting activity on various hydrophilic and hydrophobic surfaces (1,12,13,17). The extracellular products responsible for such activity were isolated and named serrawettins (lipopeptides produced by S. marcescens) (15, 16) and rubiwettins [,-D-glucopyranosyl 3-(3'-hydroxytetradecanoyloxy)decanoate and its glucosefree relatives produced by S. rubidaea] (13). Serrawettin Wi, produced by many pigmented S. marcescens strains, is a surface-active cyclodepsipeptide identical to serratamolide, which was discovered by Wasserman as an antibiotic (25, 26). Serrawettins W2 and W3 are also surface-active exolipids of nonpigmented strains of S. marcescens (W2 from strain NS 25 and W3 from strains NS 45 and NS 50). Although serrawettins W2 and W3 were identified as novel types of ninhydrin-negative lipopeptides giving protonated molecular ions at 732 and 684 mlz, respectively, in positive secondary ion mass spectra, the precise chemical structures remained unsolved. In contrast to serrawettin Wl, which has a symmetric dilactone structure composed of 2 mol of serine and 2 mol of 3-hydroxydecanoic acids (12, 26), W2 and W3 were shown to have asymmetric cyclic structures composed of several amino acids and fatty acids (14). In the present study, the chemical structure of serrawettin W2 was determined by a combination of conventional degradation analyses and nondegradation analyses such as two-dimensional nuc...

show abstract

Serratamolide, a Metabolic Product of Serratia

Cited by 78 publications

References 0 publications

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Identification and Characterization of the pswP Gene Required for the Parallel Production of Prodigiosin and Serrawettin W1 in Serratia marcescens

Mutational analysis of flagellum-independent surface spreading of Serratia marcescens 274 on a low-agar medium

A novel extracellular cyclic lipopeptide which promotes flagellum-dependent and -independent spreading growth of Serratia marcescens

Contact Info

Product

Resources

About