Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract.
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Lipid A modification systems in gram-negative bacteriaPredicting Protein Function from Structure—The Roles of Short-chain Dehydrogenase/Reductase Enzymes in Bordetella O-antigen BiosynthesisPagP Crystallized from SDS/Cosolvent Reveals the Route for Phospholipid Access to the Hydrocarbon RulerA thiolate anion buried within the hydrocarbon ruler perturbs PagP lipid acyl chain selectionInscribing the perimeter of the PagP hydrocarbon ruler by site-specific chemical alkylationMolecular basis of bacterial outer membrane permeability revisitedMolecular mechanism for lateral lipid diffusion between the outer membrane external leaflet and a beta-barrel hydrocarbon rulerStructural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membraneLipid trafficking controls endotoxin acylation in outer membranes of Escherichia coli.A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxinThe integral membrane enzyme PagP alternates between two dynamically distinct statesMicrowave-assisted sample preparation for rapid and sensitive analysis of H. pylori lipid A applicable to a single colony.A deep rough type structure in Bordetella bronchiseptica lipopolysaccharide modulates host immune responses.Shield as signal: lipopolysaccharides and the evolution of immunity to gram-negative bacteria.A rapid, small-scale procedure for the structural characterization of lipid A applied to Citrobacter and Bordetella strains: discovery of a new structural element.Glucosamine found as a substituent of both phosphate groups in Bordetella lipid A backbones: role of a BvgAS-activated ArnT orthologBordetella holmesii: Lipid A Structures and Corresponding Genomic Sequences Comparison in Three Clinical Isolates and the Reference Strain ATCC 51541.Structural modifications occurring in lipid A of Bordetella bronchiseptica clinical isolates as demonstrated by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.The Bordetella bronchiseptica type III secretion system inhibits gamma interferon production that is required for efficient antibody-mediated bacterial clearance.Bordetella pertussis pathogenesis: current and future challenges.Bordetella parapertussis PagP mediates the addition of two palmitates to the lipopolysaccharide lipid A.Review: Lipopolysaccharide biosynthesis in Pseudomonas aeruginosa.Expression of the lipopolysaccharide-modifying enzymes PagP and PagL modulates the endotoxic activity of Bordetella pertussis.Role of pagL and lpxO in Bordetella bronchiseptica lipid A biosynthesisBiosynthesis, transport, and modification of lipid A.Lipopolysaccharide heterogeneity: innate host responses to bacterial modification of lipid a structure.The PhoQ-activating potential of antimicrobial peptides contributes to antimicrobial efficacy and is predictive of the induction of bacterial resistance.Post-assembly modification of Bordetella bronchiseptica O polysaccharide by a novel periplasmic enzyme encoded by wbmE.Structural characterization of Bordetella parapertussis lipid A.Enzymatic modification of lipid A by ArnT protects Bordetella bronchiseptica against cationic peptides and is required for transmission.Interactions of pulmonary collectins with Bordetella bronchiseptica and Bordetella pertussis lipopolysaccharide elucidate the structural basis of their antimicrobial activitiesSignal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-component systems of Escherichia coli.Pertussis: a matter of immune modulation.Recognition of lipid A variants by the TLR4-MD-2 receptor complex.Fortifying the barrier: the impact of lipid A remodelling on bacterial pathogenesis.pagP is required for resistance to antibody-mediated complement lysis during Bordetella bronchiseptica respiratory infection.Species- and strain-specific control of a complex, flexible regulon by Bordetella BvgASComparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction.The BvgAS Regulon of Bordetella pertussis.Bordetella pertussis risA, but not risS, is required for maximal expression of Bvg-repressed genes.
P2860
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P2860
Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@en
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@nl
type
label
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@en
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@nl
prefLabel
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@en
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@nl
P2093
P2860
P1476
Bordetella bronchiseptica PagP ...... f the mouse respiratory tract.
@en
P2093
Andrew Preston
Duncan J Maskell
E Jane Pishko
Elinor Toland
Elizabeth Maxim
Eric T Harvill
Martine Caroff
P2860
P304
P356
10.1046/J.1365-2958.2003.03484.X
P407
P577
2003-05-01T00:00:00Z