Structure of the core oligosaccharide in the lipopolysaccharide isolated from Aeromonas salmonicida ssp. salmonicida

1992 ◽  
Vol 231 ◽  
pp. 83-91 ◽  
Author(s):  
Derek H. Shaw ◽  
M. Jeanne Hart ◽  
Otto Lüderitz
Keyword(s):  
Aeromonas Salmonicida ◽  
Core Oligosaccharide ◽  
The Core

A lipopolysaccharide-specific bacteriophage for Aeromonas salmonicida

1983 ◽  
Vol 29 (10) ◽  
pp. 1458-1461 ◽  
Author(s):  
E. E. Ishiguro ◽  
Teresa Ainsworth ◽  
D. H. Shaw ◽  
W. W. Kay ◽  
T. J. Trust
Keyword(s):  
Cell Wall ◽  
Lipid A ◽  
Aeromonas Salmonicida ◽  
Receptor Activity ◽  
Core Oligosaccharide ◽  
The Core ◽  
Phage Adsorption ◽  
Specific Bacteriophage

Cell wall lipopolysaccharide (LPS) was identified as the receptor for the Aeromonas salmonicida bacteriophage strain 55R-1. Mutants of A. salmonicida resistant to phage 55R-1 were unable to adsorb phage 55R-1 and were shown to be defective in LPS structure. Purified A. salmonicida LPS inactivated phage 55R-1, but the O-polysaccharide and the core oligosaccharide portions of the LPS were ineffective. These results suggest that lipid A was required for receptor activity. Antibodies directed against LPS also inhibited phage adsorption.

scholarly journals The Activity of Lipid A and Core Components of Bacterial Lipopolysaccharides in the Prevention of the Hypersensitive Response in Pepper

1997 ◽  
Vol 10 (7) ◽  
pp. 926-928 ◽  
Author(s):  
Mari-Anne Newman ◽  
Michael J. Daniels ◽  
J. Maxwell Dow
Keyword(s):  
Hypersensitive Response ◽  
Xanthomonas Campestris ◽  
Lipid A ◽  
Enteric Bacteria ◽  
Core Oligosaccharide ◽  
The Core ◽  
Minimal Structure ◽  
Core Components ◽  
Pre Treatment ◽  
Bacterial Lipopolysaccharides

Pre-treatment of leaves of pepper (Capsicum annuum) with lipopolysaccharide (LPS) preparations from enteric bacteria and Xanthomonas campestris could prevent the hypersensitive response caused by an avirulent X. campestris strain. By use of a range of deep-rough mutants, the minimal structure in Salmonella LPS responsible for the elicitation of this effect was determined to be lipid A attached to a disaccharide of 2-keto-3-deoxyoctulosonate; lipid A alone and the free core oligosaccharide from a Salmonella Ra mutant were not effective. For Xanthomonas, the core oligosaccharide alone had activity although lipid A was not effective. The results suggest that pepper cells can recognize different structures within bacterial LPS to trigger alterations in plant response to avirulent pathogens.

scholarly journals Structure of the core oligosaccharide of a rough-type lipopolysaccharide of Pseudomonas syringae pv. phaseolicola

2004 ◽  
Vol 271 (23-24) ◽  
pp. 4968-4977 ◽  
Author(s):  
Evelina L. Zdorovenko ◽  
Evgeny Vinogradov ◽  
Galina M. Zdorovenko ◽  
Buko Lindner ◽  
Olga V. Bystrova ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Core Oligosaccharide ◽  
The Core

Studies of the cellular and free lipopolysaccharides from Neisseria canis and N. subflava

1976 ◽  
Vol 22 (2) ◽  
pp. 189-196 ◽  
Author(s):  
K. G. Johnson ◽  
M. B. Perry ◽  
I. J. McDonald
Keyword(s):  
Single Species ◽  
Nutritional Requirements ◽  
Core Oligosaccharide ◽  
The Core ◽  
Composition And Structure ◽  
Neisseria Perflava

Cellular and free lipopolysaccharides (LPS) obtained from Neisseria canis and N. subflava were essentially identical. Both cellular and free lipopolysaccharides contained O-polysaccharides of the following composition: L-rhamnose (46 mol), D-glucose (16 mol), L-glycero-D-manno-heptose (2 mol), ethanolamine (2 mol), 3-deoxy-D-manno-octulosonic acid (1 mol), and phosphate (1.5 mol). The core oligosaccharide, which was common to the cellular and free LPS of both organisms, contained L-rhamnose (4 mol), D-glucose (2 mol), L-glycero-D-manno-heptose (2 mol), 3-deoxy-D-manno-octulosonic acid (1 mol), ethanolamine (2 mol), and phosphate (1.5 mol).Accumulated results on LPS composition and structure indicated that Neisseria perflava, N. subflava, and N. flava could not be combined into a single species. On the basis of its nutritional requirements and LPS structure, N. canis could be considered a strain of N. subflava.

Structural studies of the core region of Aeromonas salmonicida subsp. salmonicida lipopolysaccharide

2006 ◽  
Vol 341 (1) ◽  
pp. 109-117 ◽  
Author(s):  
Zhan Wang ◽  
Jianjun Li ◽  
Evgeny Vinogradov ◽  
Eleonora Altman
Keyword(s):  
Aeromonas Salmonicida ◽  
Core Region ◽  
Structural Studies ◽  
The Core

scholarly journals Investigations on the oligosaccharide units of an A myeloma globulin

1968 ◽  
Vol 107 (3) ◽  
pp. 341-352 ◽  
Author(s):  
G. Dawson ◽  
J. R. Clamp
Keyword(s):  
Sialic Acid ◽  
Electrophoretic Mobility ◽  
Acid Content ◽  
Carbohydrate Content ◽  
Glycosidic Linkage ◽  
Core Oligosaccharide ◽  
Sialic Acid Content ◽  
Acetylneuraminic Acid ◽  
The Core ◽  
Polypeptide Chains

The carbohydrate content of an A myeloma globulin was investigated. The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months. The various polymeric forms of the protein contained similar proportions of carbohydrate. The A myeloma globulin contained approx. 2 residues of 6-deoxy-l-galactose (l-fucose), 14–15 of d-mannose, 12–13 of d-galactose, 12–13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains. The oligosaccharide units showed two kinds of heterogeneity, which have been termed central and peripheral. Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2). The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid. Tentative structures are proposed for these various types of oligosaccharide unit. Glycopeptides were isolated in which the sialic acid content exceeded that of d-galactose. Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.

scholarly journals Interactions of Pulmonary Collectins with Bordetella bronchiseptica and Bordetella pertussis Lipopolysaccharide Elucidate the Structural Basis of Their Antimicrobial Activities

2004 ◽  
Vol 72 (12) ◽  
pp. 7124-7130 ◽  
Author(s):  
Lyndsay M. Schaeffer ◽  
Francis X. McCormack ◽  
Huixing Wu ◽  
Alison A. Weiss
Keyword(s):  
Bordetella Pertussis ◽  
Lipid A ◽  
Antimicrobial Activities ◽  
Innate Immune ◽  
Bordetella Bronchiseptica ◽  
Structural Basis ◽  
Wild Type ◽  
Core Oligosaccharide ◽  
The Core ◽  
O Antigen

ABSTRACT Surfactant proteins A (SP-A) and D (SP-D) play an important role in the innate immune defenses of the respiratory tract. SP-A binds to the lipid A region of lipopolysaccharide (LPS), and SP-D binds to the core oligosaccharide region. Both proteins induce aggregation, act as opsonins for neutrophils and macrophages, and have direct antimicrobial activity. Bordetella pertussis LPS has a branched core structure and a nonrepeating terminal trisaccharide. Bordetella bronchiseptica LPS has the same structure, but lipid A is palmitoylated and there is a repeating O-antigen polysaccharide. The ability of SP-A and SP-D to agglutinate and permeabilize wild-type and LPS mutants of B. pertussis and B. bronchiseptica was examined. Previously, wild-type B. pertussis was shown to resist the effects of SP-A; however, LPS mutants lacking the terminal trisaccharide were susceptible to SP-A. In this study, SP-A was found to aggregate and permeabilize a B. bronchiseptica mutant lacking the terminal trisaccharide, while wild-type B. bronchiseptica and mutants lacking only the palmitoyl transferase or O antigen were resistant to SP-A. Wild-type B. pertussis and B. bronchiseptica were both resistant to SP-D; however, LPS mutants of either strain lacking the terminal trisaccharide were aggregated and permeabilized by SP-D. We conclude that the terminal trisaccharide protects Bordetella species from the bactericidal functions of SP-A and SP-D. The O antigen and palmitoylated lipid A of B. bronchiseptica play no role in this resistance.

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