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 Outer Membrane Permeability Barrier in Escherichia coli Mutants That Are Defective in the Late Acyltransferases of Lipid A Biosynthesis

1999 ◽  
Vol 43 (6) ◽  
pp. 1459-1462 ◽  
Author(s):  
Martti Vaara ◽  
Marjatta Nurminen
Keyword(s):  
Escherichia Coli ◽  
Membrane Permeability ◽  
Outer Membrane ◽  
Lipid A ◽  
Enteric Bacteria ◽  
Normal Function ◽  
Permeability Barrier ◽  
Core Oligosaccharide ◽  
Hydrophobic Solutes ◽  
Outer Membrane Permeability

ABSTRACT The tight packing of six fatty acids in the lipid A constituent of lipopolysaccharide (LPS) has been proposed to contribute to the unusually low permeability of the outer membrane of gram-negative enteric bacteria to hydrophobic antibiotics. Here it is shown that theEscherichia coli msbB mutant, which elaborates defective, penta-acylated lipid A, is practically as resistant to a representative set of hydrophobic solutes (rifampin, fusidic acid, erythromycin, clindamycin, and azithromycin) as the parent-type control strain. The susceptibility index, i.e., the approximate ratio between the MIC for the msbB mutant and that for the parent-type control, was maximally 2.7-fold. In comparison, the rfa mutant defective in the deep core oligosaccharide part of LPS displayed indices ranging from 20 to 64. The lpxA and lpxD lipid A mutants had indices higher than 512. Furthermore, the msbBmutant was resistant to glycopeptides (vancomycin, teicoplanin), whereas the rfa, lpxA, and lpxDmutants were susceptible. The msbB htrB double mutant, which elaborates even-more-defective, partially tetra-acylated lipid A, was still less susceptible than the rfa mutant. These findings indicate that hexa-acylated lipid A is not a prerequisite for the normal function of the outer membrane permeability barrier.

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.

scholarly journals Identification of a 3-Deoxy-d-manno-Octulosonic Acid Biosynthetic Operon in Moraxella catarrhalis and Analysis of a KdsA-Deficient Isogenic Mutant

2003 ◽  
Vol 71 (11) ◽  
pp. 6426-6434 ◽  
Author(s):  
Nicole R. Luke ◽  
Simon Allen ◽  
Bradford W. Gibson ◽  
Anthony A. Campagnari
Keyword(s):  
Outer Membrane ◽  
Moraxella Catarrhalis ◽  
Lipid A ◽  
Enteric Bacteria ◽  
Isogenic Mutant ◽  
Allelic Exchange ◽  
The Core ◽  
Human Sera ◽  
Essential Enzyme

ABSTRACT Lipooligosaccharide (LOS), a predominant surface-exposed component of the outer membrane, has been implicated as a virulence factor in the pathogenesis of Moraxella catarrhalis infections. However, the critical steps involved in the biosynthesis and assembly of M. catarrhalis LOS currently remain undefined. In this study, we used random transposon mutagenesis to identify a 3-deoxy-d-manno-octulosonic acid (KDO) biosynthetic operon in M. catarrhalis with the gene order pyrG-kdsA-eno. The lipid A-KDO molecule serves as the acceptor onto which a variety of glycosyl transferases sequentially add the core and branch oligosaccharide extensions for the LOS molecule. KdsA, the KDO-8-phosphate synthase, catalyzes the first step of KDO biosynthesis and is an essential enzyme in gram-negative enteric bacteria for maintenance of bacterial viability. We report the construction of an isogenic M. catarrhalis kdsA mutant in strain 7169 by allelic exchange. Our data indicate that an LOS molecule consisting only of lipid A and lacking KDO glycosylation is sufficient to sustain M. catarrhalis survival in vitro. In addition, comparative growth and susceptibility assays were performed to assess the sensitivity of 7169kdsA11 compared to that of the parental strain. The results of these studies demonstrate that the native LOS molecule is an important factor in maintaining the integrity of the outer membrane and suggest that LOS is a critical component involved in the ability of M. catarrhalis to resist the bactericidal activity of human sera.

Complete Lipopolysaccharide ofPlesiomonas shigelloidesO74:H5 (Strain CNCTC 144/92). 2. Lipid A, Its Structural Variability, the Linkage to the Core Oligosaccharide, and the Biological Activity of the Lipopolysaccharide†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (35) ◽  
pp. 10434-10447 ◽  
Author(s):  
Jolanta Lukasiewicz ◽  
Monika Dzieciatkowska ◽  
Tomasz Niedziela ◽  
Wojciech Jachymek ◽  
Anna Augustyniuk ◽  
...  
Keyword(s):  
Biological Activity ◽  
Lipid A ◽  
Core Oligosaccharide ◽  
The Core ◽  
Structural Variability

Isolation and characterization of 3-acetamido-3,6-dideoxy-L-glucose from the core oligosaccharides obtained from the aquatic gram-negative bacteria Aeromonas hydrophila and Vibrio anguillarum

1981 ◽  
Vol 59 (11-12) ◽  
pp. 877-879 ◽  
Author(s):  
Joseph H. Banoub ◽  
Derek H. Shaw
Keyword(s):  
Aeromonas Hydrophila ◽  
Vibrio Anguillarum ◽  
Amino Sugar ◽  
Gram Negative Bacteria ◽  
Core Oligosaccharide ◽  
Gram Negative ◽  
The Core ◽  
Isolation And Characterization ◽  
Bacterial Lipopolysaccharides

The amino sugar 3-acetamido-3,6-dideoxy-L-glucose has been isolated and characterized from the core oligosaccharide obtained from the bacterial lipopolysaccharides of Aeromonas hydrophila and Vibrio anguillarum. This is the first occasion in which a dideoxyamino sugar has been confirmed as a constituent of the core oligosaccharide rather than the O-polysaccharide.

The core oligosaccharide component from Mannheimia (Pasteurella) haemolytica serotype Al lipopolysaccharide contains L-glycero-D-manno- and D-glycero-D-manno-heptoses: Analysis of the structure and conformation by high-resolution NMR spectroscopy

2002 ◽  
Vol 80 (8) ◽  
pp. 949-963 ◽  
Author(s):  
Jean-Robert Brisson ◽  
Ellen Crawford ◽  
Dušan Uhrín ◽  
Nam Huan Khieu ◽  
Malcolm B Perry ◽  
...  
Keyword(s):  
Lipid A ◽  
Inner Core ◽  
Chemical Shifts ◽  
Coupling Constants ◽  
Pasteurella Haemolytica ◽  
Core Oligosaccharide ◽  
The Core ◽  
Proton Coupling ◽  
Structure Formula ◽  
Nmr Methods

Previous studies from our laboratory have indicated that the lipopolysaccharide (LPS) from Mannheimia haemolytica serotype A1 contains both L-glycero-D-manno-heptose and D-glycero-D-manno-heptose residues. NMR methods making use of 1D 1H selective excitation and 2D (1H, 13C) and (1H, 31P) heteronuclear experiments were used for the structural determination of the major core oligosaccharide components of the deacylated low-molecular-mass LPS obtained following sequential treatment with anhydrous hydrazine and aq KOH. The core oligosaccharide region was found to be composed of a branched octasaccharide linked to the deacylated lipid A moiety via a 3-deoxy-4-phospho-D-manno-oct-2-ulosonate residue having the structure,[Formula: see text]Heterogeneity was found to be present at several linkages. NMR methods were devised to distinguish between the diastereomeric forms of the heptose residues. Synthesized monosaccharides of L-D- and D-D-heptose were used as model compounds for analysis of the 1H and 13C NMR chemical shifts and proton coupling constants. Molecular modeling using a Monte Carlo method for conformational analysis of saccharides was used to determine the conformation of the inner core of the oligosaccharide and to establish the stereochemical relationships between the heptoses.Key words: LPS, NMR, conformation, oligosaccharide, heptose.

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 Lipopolysaccharide of Yersinia Pestis, the Cause of Plague: Structure, Genetics, Biological Properties

Acta Naturae ◽  
2012 ◽  
Vol 4 (3) ◽  
pp. 46-58 ◽  
Author(s):  
Yu. A. Knirel ◽  
A. P. Anisimov
Keyword(s):  
Yersinia Pestis ◽  
Lipid A ◽  
Biological Significance ◽  
Enteric Bacteria ◽  
Biological Properties ◽  
Temperature Dependent ◽  
Core Oligosaccharide ◽  
Evolutionary Aspect ◽  
Yersinia Species ◽  
Composition And Structure

The present review summarizes data pertaining to the composition and structure of the carbohydrate moiety (core oligosaccharide) and lipid component (lipid A) of the various forms of lipopolysaccharide (LPS), one of the major pathogenicity factors of Yersinia pestis, the cause of plague. The review addresses the functions and the biological significance of genes for the biosynthesis of LPS, as well as the biological properties of LPS in strains from various intraspecies groups of Y. pestis and their mutants, including the contribution of LPS to the resistance of bacteria to factors of the innate immunity of both insect-vectors and mammal-hosts. Special attention is paid to temperature-dependent variations in the LPS structure, their genetic control and roles in the pathogenesis of plague. The evolutionary aspect is considered based on a comparison of the structure and genetics of the LPS of Y. pestis and other enteric bacteria, including other Yersinia species. The prospects of development of live plague vaccines created on the basis of Y. pestis strains with the genetically modified LPS are discussed.

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