De novo synthesis of D- and L-fucosamine containing disaccharides

The availability of rare monosaccharides that cannot be isolated from natural sources is currently limiting the access to the synthesis and the biological evaluation of complex bacterial cell-surface glycans. Here, we report the synthesis of D- and L-fucosamine building blocks by a de novo approach from L- and D-Garner aldehydes. These differentially protected monosaccharide building blocks were utilized to prepare disaccharides present on the surface of Pseudomonas aeruginosa bacteria.

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Glycogen and various other polysaccharides stimulate the formation of exolipase by Pseudomonas aeruginosa

Canadian Journal of Microbiology ◽

10.1139/m82-095 ◽

1982 ◽

Vol 28 (6) ◽

pp. 636-642 ◽

Cited By ~ 12

Author(s):

Gabriele Schulte ◽

Leuthold Bohne ◽

Ulrich Winkler

Keyword(s):

Energy Source ◽

Pseudomonas Aeruginosa ◽

Protein Synthesis ◽

Cell Surface ◽

Bacterial Cell ◽

De Novo ◽

Conditioned Media ◽

Specific Interactions ◽

Bacterial Cell Surface ◽

De Novo Protein Synthesis

Glycogen enhances the formation of exolipase by Pseudomonas aeruginosa ATCC 9027 although the cells cannot utilize it as sole carbon and energy source. Glycogen is unable to influence exolipase activities in conditioned media after removal of the cells. Treatment of cells with glycogen does not promote overall protein synthesis but inhibitors of protein synthesis (e.g., rifampicin and chloramphenicol) prevent the glycogen effect, suggesting that specific de novo protein synthesis is required. In addition to glycogen, 5 other polysaccharides (among 13 tested) were found to have exolipase-enhancing ability. The results are discussed with regard to the detachment hypothesis of U. K. Winkler and M. Stuckmann (1979. J. Bacteriol. 138: 663–670). According to this hypothesis polysaccharides are assumed to dislocate cell-bound lipase to the medium via specific interactions with the bacterial cell surface.

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De novo synthesis, structural assignment and biological evaluation of pseudopaline, a metallophore produced by Pseudomonas aeruginosa

Chemical Science ◽

10.1039/c9sc01405e ◽

2019 ◽

Vol 10 (27) ◽

pp. 6635-6641 ◽

Cited By ~ 5

Author(s):

Jian Zhang ◽

Tianhu Zhao ◽

Rongwen Yang ◽

Ittipon Siridechakorn ◽

Sanshan Wang ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Total Synthesis ◽

Natural Product ◽

Absolute Configuration ◽

De Novo ◽

Biological Evaluation ◽

De Novo Synthesis ◽

Structural Assignment ◽

The Absolute

The first total synthesis and isolation of pseudopaline was reported, which allows determination and confirmation of the absolute configuration of the natural product.

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Opsonic activity of antisera to ribosomal vaccine fractions with live and formalinized Pseudomonas aeruginosa

Canadian Journal of Microbiology ◽

10.1139/m86-098 ◽

1986 ◽

Vol 32 (6) ◽

pp. 531-533 ◽

Cited By ~ 4

Author(s):

Michael M. Lieberman ◽

Robert C. Allen

Keyword(s):

Pseudomonas Aeruginosa ◽

Cell Surface ◽

Bacterial Cell ◽

Polymorphonuclear Leukocytes ◽

Protein S ◽

Opsonic Activity ◽

Bacterial Cell Surface ◽

Ribosomal Vaccine

The opsonic capacity of antisera to Pseudomonas aeruginosa ribosomal vaccine fractions was determined by a chemiluminescent technique. Antiserum to a vaccine fraction ("peak A") containing lipopolysaccharide (antiserum A), and antiserum to a vaccine fraction ("peak B"), which did not contain detectable amounts of lipopolysaccharide (antiserum B), were used to opsonify live or formalin-treated bacteria. Polymorphonuclear leukocytes were then stimulated by the opsonified bacteria in the presence of the chemiluminigenic probe, luminol, resulting in the observed chemiluminescence. The data obtained indicated that the antisera had comparable opsonic activity with live (untreated) bacteria. However, antiserum B had far less opsonic activity than did antiserum A when formalinized bacteria were used. Owing to the effects of formaldehyde on protein, these results were interpreted as evidence to suggest that the opsonic activities of the two antisera are dependent on different antigens on the bacterial cell surface. Antiserum A activity is probably dependent on lipopolysaccharide to a great extent, whereas antiserum B activity is most likely dependent primarily on a protein(s).

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