Substrate analogues to study cell-wall biosynthesis and its inhibition

Lazar, Kristi L.; Walker, Suzanne

doi:10.1016/s1367-5931(02)00355-1

Cited by 48 publications

(34 citation statements)

References 46 publications

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“…These systems include N-linked protein glycosylation in eukaryotic (78 -80) and bacterial cells (81,82), the generation of LPS O-antigen (1), the assembly of enterobacterial common antigen (83), and the polymerization of peptidoglycan (84). Although the sugar compositions and linkages of these polyisoprene phosphate-oligosaccharides differ greatly, two common principles emerge.…”

Section: Discussionmentioning

confidence: 99%

An Undecaprenyl Phosphate-Aminoarabinose Flippase Required for Polymyxin Resistance in Escherichia coli

Yan¹,

Guan²,

Raetz

2007

Journal of Biological Chemistry

135

136

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Modification of lipid A with the 4-amino-4-deoxy-L-arabinose (L-Ara4N) moiety is required for resistance to polymyxin and cationic antimicrobial peptides in Escherichia coli and Salmonella typhimurium. An operon of seven genes (designated pmrHFIJKLM in S. typhimurium), which is regulated by the PmrA transcription factor and is also present in E. coli, is necessary for the maintenance of polymyxin resistance. We previously elucidated the roles of pmrHFIJK in the biosynthesis and attachment of L-Ara4N to lipid A and renamed these genes arn-BCADT, respectively. We now propose functions for the last two genes of the operon, pmrL and pmrM. Chromosomal inactivation of each of these genes in an E. coli pmrA c parent switched its phenotype from polymyxin-resistant to polymyxin-sensitive. The lipid A moiety of lipopolysaccharide (LPS) 4 in the outer membranes of Gram-negative bacteria typically consists of a ␤,1Ј-6-linked disaccharide of glucosamine, modified with phosphate groups at the 1-and 4Ј-positions, and with R-3-hydroxyacyl chains at the 2-, 3-, 2Ј-, and 3Ј-positions (Fig.

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Section: Discussionmentioning

confidence: 99%

An Undecaprenyl Phosphate-Aminoarabinose Flippase Required for Polymyxin Resistance in Escherichia coli

Yan¹,

Guan²,

Raetz

2007

Journal of Biological Chemistry

135

136

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“…LPS, or Schematic structure of the E. coli K-12 cell envelope. The structure and biosynthesis of LPS (2,3), peptidoglycan (186), membrane-derived oligosaccharides (239,240), lipoproteins (241), and phospholipids (242,243) are reviewed elsewhere. Strains of E. coli K-12 normally do not make O-antigen (n ∼ 1 -50), unless a mutation in the O-antigen operon is corrected (244).…”

Section: The Innate Immune Response To Lipid Amentioning

confidence: 99%

“…YeiU also functions as an undecaprenyl diphosphate phosphatase. Undecaprenyl diphosphate is generated on the outer surface of the inner membrane during the polymerization of peptidoglycan (Figure 1) (186). The lipid A diphosphate groups, synthesized by YeiU and EptA, might function to stabilize and/or balance the surface electrostatics of the outer membrane depending on environmental conditions.…”

Section: Figure 10mentioning

confidence: 99%

Lipid A Modification Systems in Gram-Negative Bacteria

Raetz

Reynolds

Trent

et al. 2007

Annu. Rev. Biochem.

1,150

1,329

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The lipid A moiety of lipopolysaccharide forms the outer monolayer of the outer membrane of most gram-negative bacteria. Escherichia coli lipid A is synthesized on the cytoplasmic surface of the inner membrane by a conserved pathway of nine constitutive enzymes. Following attachment of the core oligosaccharide, nascent core-lipid A is flipped to the outer surface of the inner membrane by the ABC transporter MsbA, where the O-antigen polymer is attached. Diverse covalent modifications of the lipid A moiety may occur during its transit from the outer surface of the inner membrane to the outer membrane. Lipid A modification enzymes are reporters for lipopolysaccharide trafficking within the bacterial envelope. Modification systems are variable and often regulated by environmental conditions. Although not required for growth, the modification enzymes modulate virulence of some gram-negative pathogens. Heterologous expression of lipid A modification enzymes may enable the development of new vaccines.

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“…Polyprenol phosphate sugars and polyprenol diphosphate sugars function in extracytoplasmic glycosylation reactions (41), in extracellular polysaccharide biosynthesis [for instance, peptidoglycan polymerization in bacteria (42)], and in eukaryotic protein N-glycosylation (43,44). The biosynthesis and function of polyprenol phosphate sugars differ significantly from those of the polyprenol diphosphate sugars; therefore, we have placed them in separate subclasses.…”

Section: Prenol Lipids [Pr]mentioning

confidence: 99%

A comprehensive classification system for lipids

Fahy

Subramaniam

Brown

et al. 2005

Journal of Lipid Research

1,433

685

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Lipids are produced, transported, and recognized by the concerted actions of numerous enzymes, binding proteins, and receptors. A comprehensive analysis of lipid molecules, "lipidomics," in the context of genomics and proteomics is crucial to understanding cellular physiology and pathology; consequently, lipid biology has become a major research target of the postgenomic revolution and systems biology. To facilitate international communication about lipids, a comprehensive classification of lipids with a common platform that is compatible with informatics requirements has been developed to deal with the massive amounts of data that will be generated by our lipid community. As an initial step in this development, we divide lipids into eight categories (fatty acyls, glycerolipids, glycerophospholipids, sphingolipids, sterol lipids, prenol lipids, saccharolipids, and polyketides) containing distinct classes and subclasses of molecules, The goal of collecting data on lipids using a "systems biology" approach to lipidomics requires the development of a comprehensive classification, nomenclature, and chemical representation system to accommodate the myriad lipids that exist in nature. Lipids have been loosely defined as biological substances that are generally hydrophobic in nature and in many cases soluble in organic solvents (1). These chemical properties cover a broad range of mole-

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Substrate analogues to study cell-wall biosynthesis and its inhibition

Cited by 48 publications

References 46 publications

An Undecaprenyl Phosphate-Aminoarabinose Flippase Required for Polymyxin Resistance in Escherichia coli

An Undecaprenyl Phosphate-Aminoarabinose Flippase Required for Polymyxin Resistance in Escherichia coli

Lipid A Modification Systems in Gram-Negative Bacteria

A comprehensive classification system for lipids

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