scholarly journals Structure of the O‐Antigen and the Lipid A from the Lipopolysaccharide of Fusobacterium nucleatum ATCC 51191

ChemBioChem ◽  
2020 ◽  
Author(s):  
Pilar Garcia‐Vello ◽  
Flaviana Di Lorenzo ◽  
Dimitra Lamprinaki ◽  
Anna Notaro ◽  
Immacolata Speciale ◽  
...  
Keyword(s):  
Lipid A ◽  
Fusobacterium Nucleatum ◽  
O Antigen

scholarly journals Evidence Suggesting That Francisella tularensis O-Antigen Capsule Contains a Lipid A-Like Molecule That Is Structurally Distinct from the More Abundant Free Lipid A

PLoS ONE ◽  
2016 ◽  
Vol 11 (6) ◽  
pp. e0157842 ◽  
Author(s):  
Jason H. Barker ◽  
Justin W. Kaufman ◽  
Michael A. Apicella ◽  
Jerrold P. Weiss
Keyword(s):  
Francisella Tularensis ◽  
Lipid A ◽  
O Antigen ◽  
Free Lipid

Structural analysis of the lipopolysaccharide O-antigen from Fusobacterium nucleatum strain CC 7/3 JVN3 C1 and development of a mouse monoclonal antibody specific to the O-antigen

2020 ◽  
Vol 66 (9) ◽  
pp. 529-534
Author(s):  
Chantelle M. Cairns ◽  
Frank St. Michael ◽  
Perry Fleming ◽  
Evgeny V. Vinogradov ◽  
Andrew D. Cox
Keyword(s):  
Colorectal Cancer ◽  
Repeat Unit ◽  
Fusobacterium Nucleatum ◽  
Cross Reactivity ◽  
Emerging Pathogen ◽  
O Antigen ◽  
Still Births ◽  
Structural Identity ◽  
Potential Factor ◽  
Surface Carbohydrates

Fusobacterium nucleatum is becoming increasingly recognised as an emerging pathogen, gaining attention as a potential factor for exacerbating colorectal cancer and is strongly linked with pregnancy complications including pre-term and still births. Little is known about the virulence factors of this organism; thus, we have initiated studies to examine the bacterium’s surface glycochemistry. In an effort to characterise the surface carbohydrates of F. nucleatum, the aims of this study were to investigate the structure of the lipopolysaccharide (LPS) O-antigen of the cancer-associated isolate F. nucleatum strain CC 7/3 JVN3 C1 (hereafter C1) and to develop monoclonal antibodies (mAbs) to the LPS O-antigen that may be beneficial to the growing field of F. nucleatum research. In this study, we combined several technologies, including nuclear magnetic resonance (NMR) spectroscopy, to elucidate the structure of the LPS O-antigen repeat unit as -[-4-β-Gal-3-α-FucNAc4N-4-α-NeuNAc-]-. We have previously identified this structure as the LPS O-antigen repeat unit from strain 10953. In this present study, we developed a mAb to the C1 LPS O-antigen and confirmed the mAbs cross-reactivity to the 10953 strain, thus confirming the structural identity.

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 Mutations in Novel Lipopolysaccharide Biogenesis Genes Confer Resistance to Amoebal Grazing in Synechococcus elongatus

2016 ◽  
Vol 82 (9) ◽  
pp. 2738-2750 ◽  
Author(s):  
Ryan Simkovsky ◽  
Emily E. Effner ◽  
Maria José Iglesias-Sánchez ◽  
Susan S. Golden
Keyword(s):  
Biomass Production ◽  
Lipid A ◽  
Synechococcus Elongatus ◽  
Cyanobacterial Blooms ◽  
Core Oligosaccharide ◽  
Diverse Range ◽  
Content Type ◽  
O Antigen ◽  
Population Structures ◽  
Pcc 7942

ABSTRACTIn natural and artificial aquatic environments, population structures and dynamics of photosynthetic microbes are heavily influenced by the grazing activity of protistan predators. Understanding the molecular factors that affect predation is critical for controlling toxic cyanobacterial blooms and maintaining cyanobacterial biomass production ponds for generating biofuels and other bioproducts. We previously demonstrated that impairment of the synthesis or transport of the O-antigen component of lipopolysaccharide (LPS) enables resistance to amoebal grazing in the model predator-prey system consisting of the heterolobosean amoeba HGG1 and the cyanobacteriumSynechococcus elongatusPCC 7942 (R. S. Simkovsky et al., Proc Natl Acad Sci U S A 109:16678–16683, 2012,http://dx.doi.org/10.1073/pnas.1214904109). In this study, we used this model system to identify additional gene products involved in the synthesis of O antigen, the ligation of O antigen to the lipid A-core conjugated molecule (including a novel ligase gene), the generation of GDP-fucose, and the incorporation of sugars into the lipid A core oligosaccharide ofS. elongatus. Knockout of any of these genes enables resistance to HGG1, and of these, only disruption of the genes involved in synthesis or incorporation of GDP-fucose into the lipid A-core molecule impairs growth. Because these LPS synthesis genes are well conserved across the diverse range of cyanobacteria, they enable a broader understanding of the structure and synthesis of cyanobacterial LPS and represent mutational targets for generating resistance to amoebal grazers in novel biomass production strains.

scholarly journals Use of Bacteriophage Ba1 To Identify Properties Associated with Bordetella avium Virulence

2002 ◽  
Vol 70 (3) ◽  
pp. 1219-1224 ◽  
Author(s):  
Celia B. Shelton ◽  
Louise M. Temple ◽  
Paul E. Orndorff
Keyword(s):  
Lipid A ◽  
Laboratory Strain ◽  
Tracheal Ring ◽  
Phage Resistance ◽  
Dependent Manner ◽  
O Antigen ◽  
Bordetella Avium ◽  
Resistant Mutants

ABSTRACT Bordetella avium causes bordetellosis, an upper respiratory disease of birds. Commercially raised turkeys are particularly susceptible. We report here on the use of a recently described B. avium bacteriophage, Ba1, as a tool for investigating the effects of lysogeny and phage resistance on virulence. We found that lysogeny had no effect on any of the in vivo or in vitro measurements of virulence we employed. However, two-thirds (six of nine) spontaneous phage-resistant mutants of our virulent laboratory strain, 197N, were attenuated. Phage resistance was associated, in all cases, with an inability of the mutants to bind phage. Further tests of the mutants revealed that all had increased sensitivities to surfactants, and increased amounts of incomplete (O-antigen-deficient) lipopolysaccharide (LPS) compared to 197N. Hot phenol-water-extracted 197N LPS inactivated phage in a specific and dose-dependent manner. Acid hydrolysis and removal of lipid A had little effect upon the ability of isolated LPS to inactivate Ba1, suggesting that the core region and possibly the O antigen were required for phage binding. All of the mutants, with one exception, were significantly more sensitive to naive turkey serum and, without exception, significantly less able to bind to tracheal rings in vitro than 197N. Interestingly, the three phage-resistant mutants that remained virulent appeared to be O antigen deficient and were among the mutants that were the most serum sensitive and least able to bind turkey tracheal rings in vitro. This observation allowed us to conclude that even severe defects in tracheal ring binding and serum resistance manifested in vitro were not necessarily indicative of attenuation and that complete LPS may not be required for virulence.

scholarly journals Loss of the WaaL O-Antigen Ligase Prevents Surface Activation of the Flagellar Gene Cascade in Proteus mirabilis

2010 ◽  
Vol 192 (12) ◽  
pp. 3213-3221 ◽  
Author(s):  
Randy M. Morgenstein ◽  
Katy M. Clemmer ◽  
Philip N. Rather
Keyword(s):  
Proteus Mirabilis ◽  
Lipid A ◽  
Response Regulator ◽  
Soft Agar ◽  
Solid Surfaces ◽  
Loss Of Function ◽  
Swarmer Cell ◽  
Gram Negative ◽  
O Antigen ◽  
Enterobacterial Common Antigen

ABSTRACT Proteus mirabilis is a Gram-negative bacterium that undergoes a physical and biochemical change from a vegetative swimmer cell (a typical Gram-negative rod) to an elongated swarmer cell when grown on a solid surface. In this study, we report that a transposon insertion in the waaL gene, encoding O-antigen ligase, blocked swarming motility on solid surfaces but had little effect on swimming motility in soft agar. The waaL mutant was unable to differentiate into a swarmer cell. Differentiation was also prevented by a mutation in wzz, encoding a chain length determinant for O antigen, but not by a mutation in wzyE, encoding an enzyme that polymerizes enterobacterial common antigen, a surface polysaccharide different from the lipid A::core. In wild-type P. mirabilis, increased expression of the flhDC operon occurs after growth on solid surfaces and is required for the high-level expression of flagellin that is characteristic of swarmer cells. However, in both the waaL and the wzz mutants, the flhDC operon was not activated during growth on agar. A loss-of-function mutation in the rcsB response regulator or overexpression of flhDC restored swarming to the waaL mutant, despite the absence of O antigen. Therefore, although O antigen may serve a role in swarming by promoting wettability, the loss of O antigen blocks a regulatory pathway that links surface contact with the upregulation of flhDC expression.

scholarly journals Biosynthesis of lipopolysaccharides with different length of the O-specific region as a virulence factor of Gram-negative bacteria

2018 ◽  
Vol 72 ◽  
pp. 573-586
Author(s):  
Eva Krzyżewska ◽  
Jacek Rybka
Keyword(s):  
Outer Membrane ◽  
Lipid A ◽  
Specific Antigen ◽  
Gram Negative Bacteria ◽  
Bacterial Survival ◽  
Core Oligosaccharide ◽  
Gram Negative ◽  
O Antigen ◽  
Length Regulation ◽  
External Part

The outer membrane of Gram-negative bacteria is a biological structure with a unique composition that significantly contributes to the survival of bacteria in the unfavorable conditions of the host organism. The lipopolysaccharide constitutes about 70% of the external part of the outer membrane. The LPS molecule is composed of three different parts: lipid A, core oligosaccharide and O antigen. Despite the O-specific antigen being one of the most intensely studied surface structures of bacterial polysaccharides, a number of questions regarding the mechanism of the O antigen biosynthesis and its transport to the cell surface are still unanswered. The paper describes the biosynthesis of the lipopolysaccharide molecule, with particular emphasis on the O-specific chain biosynthesis, the mechanism of lipopolysaccharide length regulation and the influence of the type of synthesized O-specific chains on bacterial survival in adverse host organisms.

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