Lipopolysaccharide ofRhodospirillum salinarum 40: structural studies on the core and lipid A region

1995 ◽  
Vol 164 (4) ◽  
pp. 280-289 ◽  
Author(s):  
Heike Rau ◽  
Ulrich Seydel ◽  
Marina Freudenberg ◽  
Jürgen Weckesser ◽  
Hubert Mayer
Keyword(s):  
Lipid A ◽  
Structural Studies ◽  
The Core

scholarly journals Structural studies on the core and lipid A region of a 4-amino-L-arabinose-lacking Rc-type mutant of Proteus mirabilis

1988 ◽  
Vol 172 (3) ◽  
pp. 535-541 ◽  
Author(s):  
Joanna RADZIEJEWSKA-LEBRECHT ◽  
U. Ramadas BHAT ◽  
Helmut BRADE ◽  
Hubert MAYER
Keyword(s):  
Proteus Mirabilis ◽  
Lipid A ◽  
Structural Studies ◽  
The Core ◽  
Type Mutant

Lipopolysaccharide of Rhodospirillum salinarum 40: structural studies on the core and lipid A region

1995 ◽  
Vol 164 (4) ◽  
pp. 280-289
Author(s):  
Heike Rau ◽  
Ulrich Seydel ◽  
Marina Freudenberg ◽  
Jürgen Weckesser ◽  
H. Mayer
Keyword(s):  
Lipid A ◽  
Structural Studies ◽  
The Core ◽  
Rhodospirillum Salinarum

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 A Novel 3-Deoxy-d-manno-Octulosonic Acid (Kdo) Hydrolase That Removes the Outer Kdo Sugar of Helicobacter pylori Lipopolysaccharide

2005 ◽  
Vol 187 (10) ◽  
pp. 3374-3383 ◽  
Author(s):  
Christopher Stead ◽  
An Tran ◽  
Donald Ferguson ◽  
Sara McGrath ◽  
Robert Cotter ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Lipid A ◽  
In Vitro Assay ◽  
Spectrometric Analysis ◽  
Vitro Assay ◽  
The Core ◽  
H Pylori

ABSTRACT The lipid A domain anchors lipopolysaccharide (LPS) to the outer membrane and is typically a disaccharide of glucosamine that is both acylated and phosphorylated. The core and O-antigen carbohydrate domains are linked to the lipid A moiety through the eight-carbon sugar 3-deoxy-d-manno-octulosonic acid known as Kdo. Helicobacter pylori LPS has been characterized as having a single Kdo residue attached to lipid A, predicting in vivo a monofunctional Kdo transferase (WaaA). However, using an in vitro assay system we demonstrate that H. pylori WaaA is a bifunctional enzyme transferring two Kdo sugars to the tetra-acylated lipid A precursor lipid IVA. In the present work we report the discovery of a Kdo hydrolase in membranes of H. pylori capable of removing the outer Kdo sugar from Kdo2-lipid A. Enzymatic removal of the Kdo group was dependent upon prior removal of the 1-phosphate group from the lipid A domain, and mass spectrometric analysis of the reaction product confirmed the enzymatic removal of a single Kdo residue by the Kdo-trimming enzyme. This is the first characterization of a Kdo hydrolase involved in the modification of gram-negative bacterial LPS.

THE STRUCTURES OF THE CORE-LIPID A REGIONS OF LIPOPOLYSACCHARIDES FROM SERRATIA MARCESCENS

2002 ◽  
Author(s):  
Evgeny Vinogradov ◽  
Buko Lindner ◽  
Guntram Seltmann ◽  
Joanna Radziejewska-Lebrecht ◽  
Otto Holst
Keyword(s):  
Serratia Marcescens ◽  
Lipid A ◽  
The Core ◽  
Core Lipid

scholarly journals Structural studies of lipid A from a lipopolysaccharide of the Coxiella burnetii isolate RSA 514 (Crazy)

2009 ◽  
Vol 15 ◽  
pp. 198-199 ◽  
Author(s):  
P. Vadovic ◽  
A. Fuleova ◽  
R. Ihnatko ◽  
L. Skultety ◽  
P. Halada ◽  
...  
Keyword(s):  
Coxiella Burnetii ◽  
Lipid A ◽  
Structural Studies

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 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 Structural studies on the phosphate-free lipid A of Rhodomicrobium vannielii ATCC 17100

1983 ◽  
Vol 137 (1-2) ◽  
pp. 325-332 ◽  
Author(s):  
Otto HOLST ◽  
Dietmar BOROWIAK ◽  
Jurgen WECKESSER ◽  
Hubert MAYER
Keyword(s):  
Lipid A ◽  
Structural Studies ◽  
Free Lipid ◽  
Rhodomicrobium Vannielii
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