The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides (Q27316484)

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English	The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides	scientific article

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scholarly article

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The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides (English)

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antibiotic resistance

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Mycobacterium tuberculosis

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antimicrobial resistance

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based on heuristic

inferred from title

antimicrobial peptide

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based on heuristic

inferred from title

4

object named as

Marek Fol

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7

object named as

William R Bishai

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Delphi Chatterjee

9

object named as

Delphi Chatterjee

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author name string

Erin Maloney

1

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Dorota Stankowska

2

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Jian Zhang

3

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Qi-Jian Cheng

5

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Shichun Lun

6

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Malini Rajagopalan

8

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Murty V Madiraju

10

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language of work or name

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publication date

July 2009

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5

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7

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e1000534

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copyright license

Creative Commons Attribution 4.0 International

31 July 2009

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April 2022 Public Data File from Crossref

copyright status

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A membrane protein preserves intrabacterial pH in intraphagosomal Mycobacterium tuberculosis

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Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

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The Envelope of Mycobacteria

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Biosynthesis of mycobacterial lipoarabinomannan: role of a branching mannosyltransferase

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Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice

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The Bacillus anthracis protein MprF is required for synthesis of lysylphosphatidylglycerols and for resistance to cationic antimicrobial peptides

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Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase

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Molecular mechanisms of bacterial resistance to antimicrobial peptides.

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Mycobacterium tuberculosis cells growing in macrophages are filamentous and deficient in FtsZ rings

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Mutations in the GTP-binding and synergy loop domains of Mycobacterium tuberculosis ftsZ compromise its function in vitro and in vivo

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In vivo activity of released cell wall lipids of Mycobacterium bovis bacillus Calmette-Guérin is due principally to trehalose mycolates

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The temporal expression profile of Mycobacterium tuberculosis infection in mice.

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Mycobacterium and the coat of many lipids

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28 September 2017

How do bacteria resist human antimicrobial peptides?

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28 September 2017

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

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Molecular recognition of lipid antigens by T cell receptors

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Lethal tuberculosis in interleukin-6-deficient mutant mice

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Substrate Specificity of O-L-Lysylphosphatidylglycerol Synthetase. Enzymatic Studies on the Structure of O-L-Lysylphosphatidylglycerol*

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Metabolism of Phosphatidylglycerol, Lysylphosphatidylglycerol, and Cardiolipin of Staphylococcus aureus

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The lipids of Mycobacterium tuberculosis BCG: fractionation, composition, turnover and the effects of isoniazid

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MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance.

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Regulation of the inducible acetamidase gene of Mycobacterium smegmatis

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Mycobacterial lysocardiolipin is exported from phagosomes upon cleavage of cardiolipin by a macrophage-derived lysosomal phospholipase A2.

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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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Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol

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Accelerated detection of Mycobacterium tuberculosis genes essential for bacterial survival in guinea pigs, compared with mice

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Cytochemical reaction of virulent tubercle bacilli.

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Metabolism of phosphoglycerides in Escherichia coli during growth at 37 °C and during a cold-induced lag phase

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Studies on cardiolipin biosynthesis in Mycobacterium smegmatis

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Turnover of lipids in Mycobacterium smegmatis CDC 46 and Mycobacterium phlei ATCC 354

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Complement receptor-mediated uptake and tumor necrosis factor-alpha-mediated growth inhibition of Mycobacterium tuberculosis by human alveolar macrophages

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10.1371/JOURNAL.PPAT.1000534

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