Binding of lipoteichoic acid of group A streptococci to isolated human erythrocyte membranes

Chiang, Thomas M.; Alkan, Michael; Beachey, Edwin H.

doi:10.1128/iai.26.1.316-321.1979

Cited by 24 publications

(7 citation statements)

References 19 publications

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“…properties of these adherence-mediating proteins of streptococci. Lipoteichoic acids of streptococci have been reported to bind to membranes of epithelial cells (1,4), erythrocytes (3,8), lymphocytes (2), and heart and kidney cells (12). Removal of esterified fatty acids from lipoteichoic acid by mild alkali hydrolysis destroys its membrane-binding activity (23).…”

Section: Discussionmentioning

confidence: 99%

Isolation of heart- and kidney-binding protein from group A streptococci

Stinson¹,

Bergey²

1982

Infect Immun

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Tritium-labeled, water-soluble components of Streptococcus pyogenes type M6 adsorbed to cardiac tissue in vitro. Tissue binding was time dependent, saturable, and reversible. Chromatography of the crude bacterial extract on Bio-Gel P-300 indicated a molecular weight greater than 300,000 for the heart-binding component. Sodium dodecyl sulfate (SDS) dissociated this aggregate into a protein of 18,000 to 20,000 daltons as determined by Sephacryl S-200 chromatography and SDS-polyacrylamide disc gel electrophoresis. The tissue-binding protein was also purified from streptococcal extracts by adsorption to immobilized heart components. SDS-polyacrylamide gel electrophoresis of the protein desorbed from tissue revealed a radioactive band of 19,000 daltons. Indirect immunofluorescence tests on cardiac tissue treated with streptococcal extract showed an accumulation of a bacterial antigen on the sarcolemmal sheaths. Streptococcal components also adsorbed to basement membranes of kidney. Antisera prepared to isolated cytoplasmic membranes and water-soluble extracts of S. pyogenes type M6 were the most sensitive reagents for the detection of bacterial components bound to tissue. Antisera prepared to isolated cell walls and to intact bacteria were weakly reactive in these assays.

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Section: Discussionmentioning

confidence: 99%

Isolation of heart- and kidney-binding protein from group A streptococci

Stinson¹,

Bergey²

1982

Infect Immun

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“…The lower binding affinity of LTA probably reflects the influence of the large hydrophilic polyglycerol phosphate backbone of the molecule. Furthermore, the binding of LTA (7) and palmitate (9) to erythrocyte ghosts appears to be identical.…”

Section: Resultsmentioning

confidence: 90%

“…DISCUSSION Previous studies on the membrane binding of LTA suggested that erythrocytes (5), platelets (3), lymphocytes (4), and erythrocyte ghosts (7) possess a single population of binding sites for LTA. Although it has been demonstrated that LTA can be incorporated into artificial liposomes (13), experiments with right-side-out and inside-out erythrocyte ghosts (7) have demonstrated that LTA binding sites are located primarily on the outer surface, suggesting that the direct interaction of LTA with the lipid bilayer of erythrocyte membranes is of minor importance. It may be deduced, therefore, that cell membranes possess a specific class of binding sites for LTA.…”

Section: Resultsmentioning

confidence: 99%

Fatty acid binding sites of serum albumin as membrane receptor analogs for streptococcal lipoteichoic acid

Simpson¹,

Ofek²,

Beachey³

1980

Infect Immun

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The ability of bovine serum albumin to inhibit the binding of group A streptococcal lipoteichoic acid (LTA) to human cells was investigated. Albumin blocked the ability of LTA to sensitize erythrocytes to agglutinate in the presence of anti-LTA in a dose-dependent manner. The inhibition of LTA binding to erythrocytes was demonstrated directly with radiolabeled LTA. At an albumin/ LTA molar ratio of 1.5:1, albumin binding of the radiolabged LTA to erythrocytes was inhibited by 45%. Analysis of the binding of radiolabeled LTA to erythrocytes in the presence of albumin indicated that albumin competitively inhibited the binding of LTA to putative cell membrane receptors, indicating that albumin and erythrocytes both bind to the same moiety on the LTA molecule.The lipoteichoic acids (LTA) of gram-positive bacteria are amphipathic molecules composed of linear backbone polymers of glycerol phosphate cross-linked by 1-3 phosphodiester bonds. The polyglycerol phosphate backbone is substituted to various degrees with glycosyl, alanyl, and acyl residues (for reviews, see references 10 and 15). The lipid moiety of group A streptococcal LTA is glycerophosphoryldiglucosyl diglyceride (14). Streptococcal LTA binds to a variety of cell membranes (3-6, 11), and the necessity of ester-linked fatty acids for LTA membrane binding activity was demonstrated by experiments which showed that: (i) the cleavage of ester-linked fatty acids by mild alkaline hydrolysis resulted in the loss of binding activity (5,11) and (ii) the cleaved lipid fraction of LTA inhibited the binding of the intact molecule (2). These experiments imply either the presence of a specific binding site for LTA fatty acids on the cell membrane or a nonspecific hydrophobic interaction between the fatty acids of LTA and the lipid bilayer.We have recently demonstrated that LTA, but not deacylated LTA of a similar molecular weight, binds to bovine serum albumin

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“…Displacement of 80% of labeled LTA has only been described for leukocytes (9). Other authors have found 40 to 55% displacement (2,4,8,26). The occurrence of the added unlabeled LTA in micelles may be responsible for the inability to displace all of the bound LTA (8).…”

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confidence: 99%