Lipoteichoic Acid, a Major Amphiphile of Gram-Positive Bacteria That Is Not Readily Extractable

Huff, Eskin

doi:10.1128/jb.149.1.399-402.1982

Cited by 29 publications

(15 citation statements)

References 21 publications

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“…7), deacylation products of lipoteichoic acid had not been formed, and most extracts did not contain teichoic acid. The extraction with chloroform/methanol, included by previous workers before [9][10][11][12][13]161 of after [32] phenol/water extraction, was omitted because on phenol/water extraction the membrane lipids separate into the phenol phase.…”

Section: Discussionmentioning

confidence: 99%

“…At a recent conference on bacterial surface amphiphiles it became apparent [l, 21 that there is no standard procedure for the preparation of lipoteichoic acids although these amphiphiles were discovered 13 years ago [3] and have since been shown to be membrane components of most gram-positive bacteria [4, 51. It has been generally agreed that extraction of bacteria with hot or cold aqueous phenol, which had been introduced for extraction of lipopolysaccharides from gramnegative bacteria [6], is also the most effective procedure in the case of lipoteichoic acids [I, 7,81. However the various investigators started from whole [7, 81, delipidated 19 -121, wall-depleted [13], and disrupted cells [5,, or from membrane fractions [16].…”

mentioning

confidence: 99%

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Improved Preparation of Lipoteichoic Acids

Fischer

Koch

Haas

1983

European Journal of Biochemistry

198

144

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A procedure is described for measuring the extraction of lipoteichoic acids from gram-positive bacteria in absolute terms. Virtually complete extraction was achieved from various bacteria by hot phenol/water if the cells were disrupted. Extraction of whole and delipidated cells and of the membrane fraction gave considerably lower yields.Most of the nucleic acids co-extracted from disrupted cells was removed by treatment with nucleases. Nucleaseresistant nucleic acid, protein, polysaccharide, and teichoic acid were separated from lipoteichoic acid by anionexchange chromatography on DEAE-Sephacel or hydrophobic interaction chromatography on octyl-Sepharose. Purified preparations were essentially free of polymeric contaminants, retained their alanine ester substitution, and were in the sodium salt form.Hydrophobic interaction chromatography also made it possible to recognize contamination of lipoteichoic acid with its deacylated and lyso-form, and to discriminate molecular species containing two and three, or two and four acyl groups.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Improved Preparation of Lipoteichoic Acids

Fischer

Koch

Haas

1983

European Journal of Biochemistry

198

144

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“…In contrast to this standard procedure, the cell wall teichoic acid from Bacillus subtilis DSMlO was isolated and purified as in [S]. Lipoteichoic acids were isolated by phenol extraction of disrupted cells [9] and further treated at pH 4.0 [lo]. Purification was achieved by hydrophobic interaction chromatography ([l 1,121, in preparation).…”

Section: Preparation Of Substratesmentioning

confidence: 99%

A novel glycerophosphodiesterase from Bacillus pumilus

Kusser¹,

Fiedler²

1984

FEBS Letters

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A novel glycerophosphodiesterase activity was detected in extracts from phosphate‐starved Bacillus pumilus DSM27 cells. The enzyme had a substrate specificity for glycerophosphodiester bonds and the reaction product formed with partially purified enzyme was (sn)‐glycero‐3‐phosphate. Purified cell wall teichoic acid of the polyglycerophosphate type, as well as deacylated, unsubstituted lipoteichoic acid of the polyglycerophosphate type, di(glycerophospho)glycerol (deacylated cardiolipin) and mono(glycerophospho)glycerol (deacylated phosphatidylglycerol) served as substrates for the enzyme. Their native counterparts, however, cell wall‐bound polyglycerophosphate, lipoteichoic acid (D‐alanine substitued and dealanylated), cardiolipin and phosphatiylglycerol were poor or no substrates, respectively. Enzyme activity was inhibited by purified cell walls and by heparin. The enzyme was partially purified using a column of Heparin‐Sepharose.

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“…LTA is one of the major virulence factors in the cell wall of Gram-positive bacteria, responsible for pathogenesis [11], in a way similar to LPS in Gram-negative bacteria. LTA is often released from bacteria during cell division [12], but is also liberated after bacteriolysis by neutrophil-released lysozyme or ␤-lactam antibiotics [13].…”

Section: Introductionmentioning

confidence: 99%

Lipoteichoic acid ofEnterococcus faecalisinduces the expression of chemokines via TLR2 and PAFR signaling pathways

Park

Han

Baik

et al. 2013

Journal of Leukocyte Biology

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Enterococcus faecalis is one of the most common opportunistic pathogens responsible for nosocomial infections, and its LTA is known as an important virulence factor causing inflammatory responses. As chemokines play a key role in inflammatory diseases by triggering leukocyte infiltration into the infection site, we purified EfLTA and investigated its effect on the expression of chemokines, IP-10, MIP-1α, and MCP-1, in murine macrophages. EfLTA induced the expression of these chemokines at the mRNA and protein levels. TLR2, CD14, and MyD88 were involved in the EfLTA-induced chemokine expression, as the expression was reduced remarkably in macrophages derived from TLR2-, CD14-, or MyD88-deficient mice. EfLTA induced phosphorylation of MAPKs and enhanced the DNA-binding activity of NF-κB, AP-1, and NF-IL6 transcription factors. The induction of IP-10 required ERK, JNK, p38 MAPK, PKC, PTK, PI3K, and ROS. We noticed that all of these signaling molecules, except p38 MAPK and ROS, were indispensable for the induction of MCP-1 and MIP-1α. Interestingly, the EfLTA-induced chemokine expression was mediated through PAFR/JAK/STAT1 signaling pathways without IFN-β involvement, which is different from LPS-induced chemokine expression requiring IFN-β/JAK/STAT1 signaling pathways. Furthermore, the culture supernatant of EfLTA-treated RAW 264.7 cells promoted the platelet aggregation, and exogenous PAF induced the chemokine expression in macrophages derived from WT and TLR2-deficient mice. These results suggest that EfLTA induces the expression of chemokines via signaling pathways requiring TLR2 and PAFR, which is distinct from that of LPS-induced chemokine expression.

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Lipoteichoic Acid, a Major Amphiphile of Gram-Positive Bacteria That Is Not Readily Extractable

Abstract: Commonly used procedures effected the extraction of only 10% of the lipoteichoic acid of stationary-phase cells of Staphylococcus aureus and Streptococcus faecium, unless the cells were first disrupted.

Cited by 29 publications

References 21 publications

Improved Preparation of Lipoteichoic Acids

Improved Preparation of Lipoteichoic Acids

A novel glycerophosphodiesterase from Bacillus pumilus

Lipoteichoic acid ofEnterococcus faecalisinduces the expression of chemokines via TLR2 and PAFR signaling pathways

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