Relationship of the chemical structure and immunobiological activities of lipoteichoic acid from Streptococcus faecalis (Enterococcus hirae) ATCC 9790

Tsutsui, O

doi:10.1016/0378-1097(91)90069-m

Cited by 17 publications

(27 citation statements)

References 16 publications

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“…Since the mass for LTA-10.5 is about 262 Da less than that of pre-ion-exchange LTA, it is likely that oleic acid was lost from the LTA during ion-exchange chromatography at pH 10.5. Alkali hydrolysis in 0.2 N NaOH for 2 h at 37°C removes all of the acyl groups from LTA (21,34). If LTA-10.5 had already lost oleic acid, the alkali hydrolysis would reduce the molecular weight of LTA-10.5 by only about 239 instead of 504 m/z units.…”

Section: Resultsmentioning

confidence: 99%

Monoacyl Lipoteichoic Acid from Pneumococci Stimulates Human Cells but Not Mouse Cells

Kim¹,

Seo

Han

et al. 2005

Infect Immun

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We have developed a method for obtaining pneumococcal lipoteichoic acid (LTA) with none, one, or two acyl chains. Anion-exchange chromatography at pH 9.5 yields pneumococcal LTA (labeled LTA-9.5) that has a mass spectrum identical to that of pre-ion-exchange LTA and loses 500 mass units after deacylation by alkali hydrolysis. Anion exchange at pH 10.5 produces LTA (labeled LTA-10.5) with mass peaks that are 264 mass units lower than those of pre-ion-exchange LTA, and deacylation of LTA-10.5 by alkali hydrolysis reduces the mass by only 239 mass units. This result indicates that LTA-10.5 has lost one of the two acyl chains, whereas LTA-9.5 has both acyl chains. When the biological properties of LTA-9.5 and LTA-10.5 are examined with mouse cells, only LTA-9.5 (and not LTA-10.5) is able to stimulate mouse cells to produce tumor necrosis factor alpha, interleukin-1␤, and nitric oxide. In contrast, both LTA-9.5 and LTA-10.5 can stimulate human cells. LTA became inactive when both acyl chains were removed. Thus, acyl chains are critical for LTA function, and small variations in acyl chains can alter biological properties of LTA.Lipoteichoic acid (LTA) is an important component of the cell walls of gram-positive bacteria. LTA is a polyphosphate polymer that is linked to a glycerol backbone with two acyl chains (10). The acyl chains anchor the molecule to the bacterial plasma membrane. The resulting LTA structure is amphipathic, which is also true of the lipopolysaccharide (LPS) of gram-negative bacteria. Also, like LPS, LTA is considered to be an important pathogen-associated molecular pattern capable of stimulating innate immunity and responsible for grampositive bacterial sepsis. However, the biological properties of LTA are only beginning to be elucidated because the LTA used in previous studies may have contained biologically active contaminants (12) or may have been altered in structure (25). The biological properties of LTA have been investigated mostly with staphylococcal LTA, which stimulates platelet-activating factor receptor (24) and TLR2 (9, 30). Staphylococcal LTA has been shown to induce the production of tumor necrosis factor alpha (TNF-␣) (9) and nitric oxide (NO) (7,22). It has also been shown to induce sepsis in rats when peptidoglycan is coadministered (8,23,26). Thus, staphylococcal LTA may be as important in causing gram-positive bacterial sepsis as LPS is in causing gram-negative bacterial sepsis.Along with staphylococci, pneumococci are responsible for most cases of gram-positive bacterial sepsis, which accounts for about half of all cases of bacterial sepsis (6, 35). Pneumococcal LTA has also been shown to stimulate cells via TLR2 (16,29). Yet to date, pneumococcal LTA has not been studied as extensively as has staphylococcal LTA. Also, it is difficult to extrapolate biological properties of staphylococcal LTA to those of pneumococcal LTA, since the two LTAs have significant structural differences. For instance, the polyphosphate polymer of staphylococcal LTA is composed of 20 to 50 small and va...

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Section: Resultsmentioning

confidence: 99%

Monoacyl Lipoteichoic Acid from Pneumococci Stimulates Human Cells but Not Mouse Cells

Kim¹,

Seo

Han

et al. 2005

Infect Immun

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“…LTA is a member of a class of macromolecules known as modulins, that induce a variety of proinflammatory mediators (56,98,121,160,180,214,217,255,410,477). In synergy with peptidoglycan, LTA causes septic shock and multiple organ failure (121,342,384,456,471,488).…”

Section: Role In Virulencementioning

confidence: 99%

“…Deacylation of LTA resulting in the loss of fatty acid acyl and D-alanyl substituents abolished the formation of macrophage mediators (477). Cytokine secretion in response to LTA is enhanced with cross-linking agents such as anti-poly(Gro-P) antibody (316) and the polyvalent form of poly(Gro-P)-reactive peptides (178).…”

Section: Role In Virulencementioning

confidence: 99%

A Continuum of Anionic Charge: Structures and Functions ofd-Alanyl-Teichoic Acids in Gram-Positive Bacteria

Neuhaus

Baddiley

2003

Microbiol Mol Biol Rev

905

1,097

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SUMMARY Teichoic acids (TAs) are major wall and membrane components of most gram-positive bacteria. With few exceptions, they are polymers of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and d-alanyl ester residues. Wall TA is attached to peptidoglycan via a linkage unit, whereas lipoteichoic acid is attached to glycolipid intercalated in the membrane. Together with peptidoglycan, these polymers make up a polyanionic matrix that functions in (i) cation homeostasis; (ii) trafficking of ions, nutrients, proteins, and antibiotics; (iii) regulation of autolysins; and (iv) presentation of envelope proteins. The esterification of TAs with d-alanyl esters provides a means of modulating the net anionic charge, determining the cationic binding capacity, and displaying cations in the wall. This review addresses the structures and functions of d-alanyl-TAs, the d-alanylation system encoded by the dlt operon, and the roles of TAs in cell growth. The importance of dlt in the physiology of many organisms is illustrated by the variety of mutant phenotypes. In addition, advances in our understanding of d-alanyl ester function in virulence and host-mediated responses have been made possible through targeted mutagenesis of dlt. Studies of the mechanism of d-alanylation have identified two potential targets of antibacterial action and provided possible screening reactions for designing novel agents targeted to d-alanyl-TA synthesis.

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“…[7][8][9] Lipoteichoic acid (LTA) has been reported earlier as an enterococcal PAMP recognized by host TLR2 to induce a signaling cascade that culminates in the activation of transcription factors and induction of pro-inflammatory cytokine expression. 10,11 More recent studies have, however, shown that LTA is not a TLR2 stimulant, and such perceived activation is a result of small amounts of LTA-associated lipoproteins in these preparations that bind to TLR2. 12,13 Other studies have suggested earlier that the host can employ TLR2-independent pathways to stimulate inflammatory cascades during Gram-positive bacterial infection, 14 implying that in addition to lipoproteins, there could be other enterococcal virulence factors participating in stimulating the inflammatory response.…”

Section: Introductionmentioning

confidence: 99%

Surface protein Esp enhances pro-inflammatory cytokine expression through NF-κB activation during enterococcal infection

Zou

Shankar

2015

Innate Immun

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Enterococcal surface protein (Esp) is encoded on a pathogenicity island in Enterococcus faecalis and E. faecium and is involved in biofilm formation and binding to epithelial cells. In this study, using Esp-expressing E. faecalis MMH594 and its isogenic Esp-deficient strain, as well as purified Esp, we show that Esp is sufficient for activation of NF-kB and the subsequent production of pro-inflammatory cytokines IL-1b and TNF-a in macrophages in vitro. In a mouse peritonitis model, we also show that mice infected with Esp-expressing E. faecalis showed comparatively higher levels of cytokines TNF-a, IL-1b and IL-6 in peritoneal fluid, and IL-6 in serum. Moreover, neutrophil infiltration and tissue damage in the liver was higher in the mice infected with the Esp-expressing strain compared with mice infected with the Esp-deficient mutant. These results add Esp to the growing list of enterococcal virulence factors that can modulate inflammation during infection and has implications for enterococcal pathogenesis.

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Relationship of the chemical structure and immunobiological activities of lipoteichoic acid from Streptococcus faecalis (Enterococcus hirae) ATCC 9790

Cited by 17 publications

References 16 publications

Monoacyl Lipoteichoic Acid from Pneumococci Stimulates Human Cells but Not Mouse Cells

Monoacyl Lipoteichoic Acid from Pneumococci Stimulates Human Cells but Not Mouse Cells

A Continuum of Anionic Charge: Structures and Functions ofd-Alanyl-Teichoic Acids in Gram-Positive Bacteria

Surface protein Esp enhances pro-inflammatory cytokine expression through NF-κB activation during enterococcal infection

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