MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing. - Wikidata - awgldk - TriplyDB

MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing.

MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing.

http://www.wikidata.org/entity/Q39707027

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Keratinocyte production of cathelicidin provides direct activity against bacterial skin pathogens Human neutrophils kill Bacillus anthracis Antimicrobial Mechanisms of Macrophages and the Immune Evasion Strategies of Staphylococcus aureus Antimicrobial Peptides Targeting Gram-Positive Bacteria Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion.Modular determinants of antimicrobial activity in platelet factor-4 family kinocidins.Transcriptome analysis of the responses of Staphylococcus aureus to antimicrobial peptides and characterization of the roles of vraDE and vraSR in antimicrobial resistance.Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol.Colonization and infection of the skin by S. aureus: immune system evasion and the response to cationic antimicrobial peptides.LysPGS formation in Listeria monocytogenes has broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance.Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus.DltABCD- and MprF-mediated cell envelope modifications of Staphylococcus aureus confer resistance to platelet microbicidal proteins and contribute to virulence in a rabbit endocarditis model.Role of mprF1 and mprF2 in the pathogenicity of Enterococcus faecalis.Antimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria.The msaABCR operon regulates resistance in vancomycin-intermediate Staphylococcus aureus strains.Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus.Analysis of the effects of cigarette smoke on staphylococcal virulence phenotypes Candidate targets of balancing selection in the genome of Staphylococcus aureus Bacterial Evasion of Host Antimicrobial Peptide Defenses Staphylococcus aureus evasion of innate antimicrobial defense.Bacterial sensing of antimicrobial peptides.Analysis of the Staphylococcus aureus abscess proteome identifies antimicrobial host proteins and bacterial stress responses at the host-pathogen interface.Innate barriers against infection and associated disorders.Broad-spectrum antimicrobial peptide resistance by MprF-mediated aminoacylation and flipping of phospholipids.Bacterial resistance mechanisms against host defense peptides.Bacterial resistance to cationic antimicrobial peptides.The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.Surface-localized spermidine protects the Pseudomonas aeruginosa outer membrane from antibiotic treatment and oxidative stress.Protein aggregation as an antibiotic design strategy.D-alanylation of teichoic acids promotes group a streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion.Regulation of mprF by antisense RNA restores daptomycin susceptibility to daptomycin-resistant isolates of Staphylococcus aureus Analysis of cell membrane characteristics of in vitro-selected daptomycin-resistant strains of methicillin-resistant Staphylococcus aureus.CpsY influences Streptococcus iniae cell wall adaptations important for neutrophil intracellular survival.Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances.Immunological control of methicillin-resistant Staphylococcus aureus (MRSA) infection in an immunodeficient murine model of thermal injuries.Envelope Structures of Gram-Positive Bacteria.The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes.

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P2860

MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing.

http://www.wikidata.org/entity/Q39707027

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2003 nî lūn-bûn

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2003年の論文

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name

MprF-mediated lysinylation of ...... ndependent neutrophil killing.

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MprF-mediated lysinylation of ...... ndependent neutrophil killing.

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MprF-mediated lysinylation of ...... ndependent neutrophil killing.

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MprF-mediated lysinylation of ...... ndependent neutrophil killing.

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MprF-mediated lysinylation of ...... ndependent neutrophil killing.

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MprF-mediated lysinylation of ...... ndependent neutrophil killing.

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IAI.71.1.546-549.2003

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Infection and Immunity

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MprF-mediated lysinylation of ...... independent neutrophil killing

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Andreas Peschel

http://www.w3.org/2001/XMLSchema#string

Birgid Neumeister

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Manuela Dürr

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Sascha A Kristian

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P2860

Antimicrobial peptides of multicellular organisms

Cathelicidins: a family of endogenous antimicrobial peptides

Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides.

Innate antimicrobial peptide protects the skin from invasive bacterial infection.

Defensins of vertebrate animals.

Staphylococcal resistance to antimicrobial peptides of mammalian and bacterial origin.

How do bacteria resist human antimicrobial peptides?

Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine

The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes.

Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils.

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546-549

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10.1128/IAI.71.1.546-549.2003

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1

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71

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Jos A. G. Van Strijp

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12496209

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143157

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