Bacterial lipopolysaccharides—Themes and variations

Wilkinson, Stephen G.

doi:10.1016/s0163-7827(96)00004-5

Cited by 152 publications

(149 citation statements)

References 693 publications

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“…1, the terminal GlcN residue in C. jejuni lipid A is replaced with 3 0 -amino-3 0 -deoxy-D-glucosamine (GlcN3N). Four primary acyl chains are linked to the disaccharide in 2-, 3-, 2 0 -, and 3 0 -positions, and two secondary acyl chains are esterified to the hydroxyl groups of the 2 0 -, and 3 0 -primary acyl chains, i.e., C2 C 14 (3-OH), C3 C 14 (3-OH), C2 0 C 14 (3-OH) and a secondary ester-linked C 16 , and C3 0 C 14 (3-OH) and a secondary ester-linked C 16 (14,15). In this study, C. jejuni lipid A is denoted as CJ-A.…”

Section: Methodsmentioning

confidence: 99%

“…In hepta-acylated lipid A, four primary acyl chains are directly linked to sugars in the 2-, 3-, 2 0 -, and 3 0 -positions. Three secondary acyl chains are ester-linked to the 2-, 3-, and 3 0 -primary acyl chains, i.e., C2 C 14 (3-OH) and a secondary ester-linked C 16 , C3 C 14 (3-OH), C2 0 C 14 (3-OH) and a secondary ester-linked C 14 , and C3 0 C 14 (3-OH) and a secondary ester-linked C 14 . The hexa-acylated lipid A form is the same as the hepta-acylated form, but there is no secondary C 16 in the 2-position (24,25).…”

Section: Methodsmentioning

confidence: 99%

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Bilayer Properties of Lipid A from Various Gram-Negative Bacteria

Kim

Patel

Park

et al. 2016

Biophysical Journal

132

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Lipid A is the lipid anchor of a lipopolysaccharide in the outer leaflet of the outer membrane of Gram-negative bacteria. In general, lipid A consists of two phosphorylated N-acetyl glucosamine and several acyl chains that are directly linked to the two sugars. Depending on the bacterial species and environments, the acyl chain number and length vary, and lipid A can be chemically modified with phosphoethanolamine, aminoarabinose, or glycine residues, which are key to bacterial pathogenesis. In this work, homogeneous lipid bilayers of 21 distinct lipid A types from 12 bacterial species are modeled and simulated to investigate the differences and similarities of their membrane properties. In addition, different neutralizing ion types (Ca 2þ , K þ , and Na þ ) are considered to examine the ion's influence on the membrane properties. The trajectory analysis shows that (1) the area per lipid is mostly correlated to the acyl chain number, and the area per lipid increases as a function of the acyl chain number; (2) the hydrophobic thickness is mainly determined by the average acyl chain length with slight dependence on the acyl chain number, and the hydrophobic thickness generally increases with the average acyl chain length; (3) a good correlation is observed among the area per lipid, hydrophobic thickness, and acyl chain order; and (4) although the influence of neutralizing ion types on the area per lipid and hydrophobic thickness is minimal, Ca 2þ stays longer on the membrane surface than K þ or Na þ , consequently leading to lower lateral diffusion and a higher compressibility modulus, which agrees well with available experiments.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Bilayer Properties of Lipid A from Various Gram-Negative Bacteria

Kim

Patel

Park

et al. 2016

Biophysical Journal

132

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“…Many reviews are available on the structure, biosynthesis, and genetic determination of LPS (262,(526)(527)(528)594), including an extensive review with 810 references, emphasizing structure (735). A recent and comprehensive review discusses LPS structure and biosynthesis in detail (529).…”

Section: General Structure Of Lpsmentioning

confidence: 99%

“…10A). Although E. coli K-12 cannot synthesize the O chain because of an insertion mutation (634) and thus produces a "rough" or Rtype LPS devoid of O chains, most wild-type strains of members of the Enterobacteriaceae synthesize this outermost structure of LPS, which often consists of oligosaccharide repeating units (735).…”

Section: General Structure Of Lpsmentioning

confidence: 99%

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

Nikaido

2003

Microbiol Mol Biol Rev

3,768

3,800

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Gram-negative bacteria characteristically are surrounded by an additional membrane layer, the outer membrane. Although outer membrane components often play important roles in the interaction of symbiotic or pathogenic bacteria with their host organisms, the major role of this membrane must usually be to serve as a permeability barrier to prevent the entry of noxious compounds and at the same time to allow the influx of nutrient molecules. This review summarizes the development in the field since our previous review (H. Nikaido and M. Vaara, Microbiol. Rev. 49:1-32, 1985) was published. With the discovery of protein channels, structural knowledge enables us to understand in molecular detail how porins, specific channels, TonB-linked receptors, and other proteins function. We are now beginning to see how the export of large proteins occurs across the outer membrane. With our knowledge of the lipopolysaccharide-phospholipid asymmetric bilayer of the outer membrane, we are finally beginning to understand how this bilayer can retard the entry of lipophilic compounds, owing to our increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopolysaccharide structure is modified by environmental conditions

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“…Unlike enteric Gram-negative bacteria, Haemophilus, Bordetella, Moraxella, and Neisseria species synthesize a form of LPS containing an oligosaccharide linked to lipid A without repeating subunit O-Ag polysaccharide chains (referred to as lipooligosaccharide or LOS) (42,43). H. influenzae LOS is highly hydrophobic, and its biochemical characteristics may limit permeability through the membranes we tested.…”

Section: H Influenzae Los Does Not Induce Icam-1 Expression On Respimentioning

confidence: 99%

Haemophilus influenzaeStimulates ICAM-1 Expression on Respiratory Epithelial Cells

Frick¹,

Joseph²,

Pang³

et al. 2000

The Journal of Immunology

119

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Epithelial cells interact directly with bacteria in the environment and play a critical role in airway defense against microbial pathogens. In this study, we examined the response of respiratory epithelial cells to infection with nontypable Haemophilus influenzae. Using an in vitro cell culture model, we found that epithelial cell monolayers released significant quantities of IL-8 and expressed increased levels of ICAM-1 mRNA and surface protein in response to H. influenzae. In contrast, levels of IL-1β, TNF-α, and MHC class I were not significantly affected, suggesting preferential activation of a specific subset of epithelial genes directed toward defense against bacteria. Induction of ICAM-1 required direct bacterial interaction with the epithelial cell surface and was not reproduced by purified H. influenzae lipooligosaccharide. Consistent with a functional role for this response, induction of ICAM-1 by H. influenzae mediated increased neutrophil adherence to the epithelial cell surface. Furthermore, in an in vivo murine model of airway infection with H. influenzae, increased epithelial cell ICAM-1 expression coincided with increased chemokine levels and neutrophil recruitment in the airway. These results indicate that ICAM-1 expression on human respiratory epithelial cells is induced by epithelial cell interaction with H. influenzae and suggest that an ICAM-1-dependent mechanism can mediate neutrophil adherence to these cells independent of inflammatory mediator release by other cell types. Direct induction of specific epithelial cell genes (such as ICAM-1 and IL-8) by bacterial infection may allow for rapid and efficient innate defense in the airway.

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Bacterial lipopolysaccharides—Themes and variations

Cited by 152 publications

References 693 publications

Bilayer Properties of Lipid A from Various Gram-Negative Bacteria

Bilayer Properties of Lipid A from Various Gram-Negative Bacteria

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

Haemophilus influenzaeStimulates ICAM-1 Expression on Respiratory Epithelial Cells

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