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

1982 ◽  
Vol 28 (6) ◽  
pp. 636-642 ◽  
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.

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

2013 ◽  
Vol 9 ◽  
pp. 332-341 ◽  
Author(s):  
Daniele Leonori ◽  
Peter H Seeberger
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Surface ◽  
Bacterial Cell ◽  
De Novo ◽  
Building Blocks ◽  
Biological Evaluation ◽  
De Novo Synthesis ◽  
Natural Sources ◽  
Bacterial Cell Surface ◽  
Cell Surface Glycans

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.

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

1986 ◽  
Vol 32 (6) ◽  
pp. 531-533 ◽  
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).

Fe(iii)-complex mediated bacterial cell surface immobilization of eGFP and enzymes

2021 ◽  
Author(s):  
Lilin Feng ◽  
Liang Gao ◽  
Daniel F. Sauer ◽  
Yu Ji ◽  
Haiyang Cui ◽  
...  
Keyword(s):  
Cell Surface ◽  
Bacterial Cell ◽  
Surface Immobilization ◽  
E Coli ◽  
Bacterial Cell Surface ◽  
Reversible Method

A facile and reversible method to immobilize His6-tagged proteins on the E. coli cell surface through the formation of an Fe(iii)-complex.

scholarly journals Viral Gene Expression Patterns in Human Herpesvirus 6B-Infected T Cells

2002 ◽  
Vol 76 (15) ◽  
pp. 7578-7586 ◽  
Author(s):  
Bodil Øster ◽  
Per Höllsberg
Keyword(s):  
Gene Expression ◽  
T Cells ◽  
Protein Synthesis ◽  
De Novo ◽  
Expression Patterns ◽  
Human Herpesvirus ◽  
Viral Gene Expression ◽  
Polymerase Activity ◽  
Viral Gene ◽  
De Novo Protein Synthesis

ABSTRACT Herpesvirus gene expression is divided into immediate-early (IE) or α genes, early (E) or β genes, and late (L) or γ genes on the basis of temporal expression and dependency on other gene products. By using real-time PCR, we have investigated the expression of 35 human herpesvirus 6B (HHV-6B) genes in T cells infected by strain PL-1. Kinetic analysis and dependency on de novo protein synthesis and viral DNA polymerase activity suggest that the HHV-6B genes segregate into six separate kinetic groups. The genes expressed early (groups I and II) and late (groups V and VI) corresponded well with IE and L genes, whereas the intermediate groups III and IV contained E and L genes. Although HHV-6B has characteristics similar to those of other roseoloviruses in its overall gene regulation, we detected three B-variant-specific IE genes. Moreover, genes that were independent of de novo protein synthesis clustered in an area of the viral genome that has the lowest identity to the HHV-6A variant. The organization of IE genes in an area of the genome that differs from that of HHV-6A underscores the distinct differences between HHV-6B and HHV-6A and may provide a basis for further molecular and immunological analyses to elucidate their different biological behaviors.

De novo protein synthesis in relation to ammonia and proline accumulation in water stressed white clover

2004 ◽  
Vol 31 (8) ◽  
pp. 847 ◽  
Author(s):  
Tae-Hwan Kim ◽  
Bok-Rye Lee ◽  
Woo-Jin Jung ◽  
Kil-Yong Kim ◽  
Jean-Christophe Avice ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Water Deficit ◽  
White Clover ◽  
De Novo ◽  
Proline Accumulation ◽  
Leaf Water ◽  
Total N ◽  
Water Parameters ◽  
Leaves And Roots ◽  
De Novo Protein Synthesis

The kinetics of protein incorporation from newly-absorbed nitrogen (N, de novo protein synthesis) was estimated by 15N tracing in 18-week-old white clover plants (Trifolium repens L. cv. Regal) during 7 d of water-deficit treatment. The physiological relationship between kinetics and accumulation of proline and ammonia in response to the change in leaf-water parameters was also assessed. All leaf-water parameters measured decreased gradually under water deficit. Leaf and root dry mass was not significantly affected during the first 3 d when decreases in leaf-water parameters were substantial. However, metabolic parameters such as total N, proline and ammonia were significantly affected within 1 d of commencement of water-deficit treatment. Water-deficit treatment significantly increased the proline and NH3–NH4+ concentrations in both leaves and roots. There was a marked reduction in the amount of N incorporated into the protein fraction from the newly absorbed N (NANP) in water-deficit stressed plants, particularly in leaf tissue. This reduction in NANP was strongly associated with an increased concentration of NH3–NH4+ in roots (P≤0.05) and proline (P≤0.01) in leaves and roots. These results suggest that proline accumulation may be a sensitive biochemical indicator of plant water status and of the dynamics of de novo protein synthesis in response to stress severity.

scholarly journals Facile method to stain the bacterial cell surface for super-resolution fluorescence microscopy

The Analyst ◽  
2014 ◽  
Vol 139 (12) ◽  
pp. 3174-3178 ◽  
Author(s):  
Ian L. Gunsolus ◽  
Dehong Hu ◽  
Cosmin Mihai ◽  
Samuel E. Lohse ◽  
Chang-soo Lee ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Cell Surface ◽  
Bacterial Cell ◽  
Super Resolution ◽  
Bacterial Cell Surface

The Bacterial Cell Surface in Relation to the Environment

1984 ◽  
pp. 194-219
Author(s):  
Stephen M. Hammond ◽  
Peter A. Lambert ◽  
Andrew N. Rycroft
Keyword(s):  
Cell Surface ◽  
Bacterial Cell ◽  
Bacterial Cell Surface
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