Surface protein of a Streptococcus agalactiae isolate

Cueninck, B J De

doi:10.1128/iai.24.3.637-641.1979

Cited by 5 publications

(2 citation statements)

References 17 publications

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“…Binding studies. Binding of radiolabeled fibrinogen to 60 beta-hemolytic group B and 40 group D streptococcal strains was measured in a standardized assay by using 0.4 jig of labeled protein added to 4 x 105 bacterial cells. In this assay fibrinogen was found to bind to 6 of 60 group B strains studied (strains SB1, SB2, SB3, SB35, SB55, and SB60; Fig.…”

Section: Resultsmentioning

confidence: 99%

Receptors for fibrinogen and aggregated beta 2-microglobulin detected in strains of group B streptococci

Schönbeck¹,

Björck²,

Kronvall³

1981

Infect Immun

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Binding of radiolabeled human fibrinogen and aggregated beta-microglobulin was measured in 60 strains of beta-hemolytic group B streptococci. Positive fibrinogen binding was detected in seven of the strains. Six of the group B strains showed an uptake of aggregated beta 2-microglobulin. Four individual strains carried both receptors, indicating a positive correlation between their occurrence. Inhibition studies showed that fibrinogen competed sterically with beta 2-microglobulin binding. Receptors for both proteins were trypsin sensitive. The presence of receptors did not correlate with the serological type of the 49 group B strains tested. However, all seven type II strains were negative. No uptake of fibrinogen was noted in any of 40 group D strains tested. Binding structures for fibrinogen and aggregated beta 2-microglobulin detected in group B streptococci were similar to receptors for the same proteins in group A, C, and G streptococci in terms of mutual correlation and steric interference of binding. The occasional occurrence of these receptors also in group B strains might reflect a common origin of some types of surface proteins in gram-positive cocci.

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Section: Resultsmentioning

confidence: 99%

Receptors for fibrinogen and aggregated beta 2-microglobulin detected in strains of group B streptococci

Schönbeck¹,

Björck²,

Kronvall³

1981

Infect Immun

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“…Although useful taxonomically, the function of these proteins has not been described. A 31-kd surface protein has also been reported in group B streptococci (13), and three proteins, of unknown function, have been found in S. mutans (32).…”

Section: Discussionmentioning

confidence: 99%

Cell surface proteins of oral streptococci

Appelbaum¹,

Rosan²

1984

Infect Immun

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Whole cells of representative strains of oral streptococci (Streptococcus sanguis, S. mitis, and S. salivarius) were radiolabeled by the lactoperoxidase method of radioiodination. The labeled polypeptides obtained by extraction of whole cells with boiling sodium dodecyl sulfate were analyzed by polyacrylamide gel electrophoresis and autoradiography. Of the total radioactivity, ca. 70% was released by treating whole cells with trypsin, suggesting that the labeling was confined to proteins located on the cell surface. Most S. sanguis strains studied gave a characteristic banding pattern consisting of a high-molecular-weight (120,000 [120K] to 63K) group of six proteins. Three low-molecular-weight (12K, 16K, and 18K) proteins were also detected in many strains.

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Isolation and properties of a novel IgG-binding protein from streptococci of serological group U

Chhatwal

Blobel

1987

Med Microbiol Immunol

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A nonimmune binding of immunoglobulin (Ig) G has been detected in streptococci of group U. The group U Fc-binding site differed from the five previously known types of staphylococcal and streptococcal Fc-binding sites by its strong affinity for murine IgG, with dissociation constants in nanomolar range for rat and mouse IgG, as well as for mouse IgG subclasses 1, 2a, 2b and 3. It also differed from other binding sites by the high sensitivity towards trypsin. The Fc-binding protein could be solubilized from the streptococci of group U with papain and purified by gel filtration on sephacryl S-200 and by subsequent affinity chromatography on human IgG-Sepharose. The purified binding protein was homogeneous on SDS-polyacrylamide gel electrophoresis and had a molecular weight of approximately 58,000 daltons. It retained its binding activities for murine IgG subclasses as revealed by western blotting. Coupled to CNBr-activated sepharose, the purified Fc-binding protein could be effectively used for the isolation of murine IgG subclasses by affinity chromatography.

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Surface protein of a Streptococcus agalactiae isolate

Cited by 5 publications

References 17 publications

Receptors for fibrinogen and aggregated beta 2-microglobulin detected in strains of group B streptococci

Receptors for fibrinogen and aggregated beta 2-microglobulin detected in strains of group B streptococci

Cell surface proteins of oral streptococci

Isolation and properties of a novel IgG-binding protein from streptococci of serological group U

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