The Nature of Secretory Agglutinins and Aggregating Factors

Eggert, Michael

doi:10.1159/000232481

Cited by 8 publications

(28 citation statements)

References 10 publications

(10 reference statements)

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“…It was heat stable at 90:'C whereas secretory IgA is not [25] and, as shown earlier [9], the agglutinin reacting with Streptococcus rnutuns T H 16 requires calcium ions to be active while secretory IgA does not. The agglutinin subunit had a molecular weight of the same order as secretory IgA but the agglutinin band in the SDS/polyacrylamide gel electrophoresis did not show identity to the secretory IgA run in parallel.…”

Section: Discussionsupporting

confidence: 51%

“…The main difference is a lower proline and a higher serine and threonine content in the agglutinin. Eggert [25] reported a heat stability for his salivary agglutinin up to 60°C for 30 min, whereas in this study agglutinin could tolerate 90 'C for 30 min without any noteworthy loss of aggregating activity. The divergences in results indicate that the studied preparations differ in composition.…”

Section: Discussionmentioning

confidence: 54%

“…This value seems low. In another study [25] a value of 60 -90 S is reported for bacteria-agglutinating salivary glycoproteins. A calcium dependence for the agglutinins was reported which is in agreement with the findings in this and in earlier studies [9, 261. The positive response of the purified agglutinin to anti-(secretory IgA) seems to indicate that secretory IgA could be included in the complex as a minor contaminant.…”

Section: Discussionmentioning

confidence: 87%

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Characterization of a Salivary Agglutinin Reacting with a Serotype c Strain of Streptococcus mutans

Ericson

Rundegren

1983

European Journal of Biochemistry

161

153

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A protein, which can agglutinate a Streptococcus mutans serotype c strain, was isolated from parotid saliva by affinity adsorption of the salivary agglutinin to the microorganism followed by a desorption with a 10 mM phosphate buffer. The agglutinin was subjected to preparative ultracentrifugation, gel filtration, and ultrafiltration. The native purified agglutinin is active only in the presence of Ca. Polyacrylamide gel electrophoresis, analytical centrifugation, and analyses of amino acids and carbohydrates showed that the native agglutinin was a fucose-rich glycoprotein with a carbohydrate content of 45 % and with a molecular weight of at least 5 x lo6. After sodium dodecyl sulphate treatment the molecular weight was 4.4 x 10'. There was a low content of proline and a high content of aspartic acid, serine and threonine. The concentration of agglutinin in parotid saliva is less than 0.5 % of total protein. It has high biological activity: 0.1 pg agglutinin causes a rapid aggregation of approximately lo8 bacteria.The compositions of secretions produced by different exocrine cells in various mucosal tissues are remarkably alike. The characteristics are the presence of potentially antibacterial systems, like secretory IgA, lactoperoxidase, lactoferrin and lysozyme, as well as of high-molecular-weight glycoproteins, which traditionally have been ascribed the role of lubricants. However, it has become evident that some of the highmolecular-weight glycoproteins also carry antibacterial properties [I, 21. Like secretory IgA, and under some conditions lysozyme also, they serve as bacterial agglutinins.The high-molecular-weight glycoproteins bind to surface receptor sites on microorganisms and under certain conditions they cause aggregation of microorganisms [2]. Aggregation or mere coating of microorganisms by salivary bacteriaaggregating glycoproteins or secretory IgA is suggested to contribute to the elimination of microorganisms from the oral cavity by blocking attachment sites on the bacterial surface. It has been suggested [I] that similarity in chemical structure between soluble glycoproteins and epithelial surface receptors, which recognize bacteria, would give rise to an intersepting mechanism, which prevents the bacteria from becoming attached to the epithelial surface.On the other hand, agglutinins, incorporated in the glycoprotein coat of the mucosa or in the acquired pellicle of the tooth surface, may favour attachment of bacteria [I, 3, 41. The balance between clearance and attachment of bacteria results in a selection of the bacteria colonizing the different surfaces [l -3, 51. It is, therefore, of prime interest to study the selecting mechanisms leading to retention of pathogenic microorganisms.In the present study we have isolated and characterized a glycoprotein which agglutinates a serotype c strain of Streptococcus mutans. Serotype c strains of S. mutam are recognized as cariogenic (for review see [6] significance of and some characteristics for the agglutinin specific for these strains have been de...

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Section: Discussionsupporting

confidence: 51%

Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 87%

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Characterization of a Salivary Agglutinin Reacting with a Serotype c Strain of Streptococcus mutans

Ericson

Rundegren

1983

European Journal of Biochemistry

161

153

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“…In other studies, Kuhlman et al (13) showed that serum MBP binds to mannose-rich 0-poly-+ Adsorbed BAL saccharides on the surface ofwild-type Salmonella montevideo ;orbance 1.0 has been extensively studied in the context of oral microbes BAL or with 3 and saliva (22,31), and there appear to be several types of affinity chrosalivary proteins that can mediate bacterial agglutination. e was adjusted Among these is a group of nonimmunoglobulin, nonmucous ubations were salivary agglutinins with conglutinin-like activity (32,33 (3) and are also consistent with protein biochemical studies that indie calcium-in-cate that SP-D is assembled as tetramers of trimers, similar to )served sugar bovine conglutinin (2,4). Although there are differences in th SP-D and apparent carbohydrate specificity (3), both proteins can also iich are effecmediate complement-dependent erythrocyte agglutination s (30 The efficient labeling of LPS from Rc and Rd mutants (but not from Re mutants or lipid A) and the efficient inhibition of Y1088 agglutination by Rc-LPS strongly implicate core terminal glucose and/or heptose residues in SP-D binding to LPS.…”

Section: Discussionmentioning

confidence: 99%

Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage.

Kuan¹,

Rust²,

Crouch³

1992

J. Clin. Invest.

297

221

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Kd of 2 X 10-11 M. At higher concentrations, SP-D also caused Ca"+-dependent agglutination of Y1088 that was inhibited by a-glucosyl-containing saccharides, antisera to the carbohydrate-binding domain of SP-D, or Y1088 LPS. Lectin blots showed specific binding of 125I-SP-D to Y1088 LPS, as well as LPS from other several strains of enteric Gram-negative bacteria. Immunogold studies demonstrated strong and uniform surface labeling of the bacteria. Rat and human bronchoalveolar lavage (BAL) caused Ca++-dependent agglutination of E. coli that was dose dependent and inhibited by competing saccharides or anti-SP-D. SP-D was selectively and efficiently adsorbed from rat BAL by incubation with E. coli, and incubation of E. coli with radiolabeled rat type II cell medium revealed that SP-D is the major E. coli-binding protein secreted by freshly isolated cells in culture. We suggest that SP-D plays important roles in the lung's defense against Gram-negative bacteria. (J. Clin. Invest. 1992. 90:97-106.)

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“…These EDTA-sensitive factors are also distinguished from 1 IS IgA by their large molecular size [Hay et al, 1971;Lachmann and Thompson, 1970] be tween 60S and 90S [Eggert, 1977[Eggert, , 1979a.…”

Section: Introductionmentioning

confidence: 99%

The Nature of Secretory Agglutinins and Aggregating Factors

Eggert¹

1980

Int Arch Allergy Immunol

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Secretory conglutinin-like factor (SKF), secretory bacterial aggregating factors (SBAF) and 11S secretory IgA antibodies of human saliva and full term amniotic fluid were quantitated by microtitration and partially characterized. The SBAF of both saliva and amniotic fluid aggregated a variety of oral streptococci, but no secretory IgA antibodies were found in amniotic fluid. The SKF and SBAF are distinguished from IIS IgA antibodies by being inhibited with EDTA and by being more susceptible to inhibition with reducing agents. These active factors are also distinguished from submaxillary mucins. Components of normal serum inhibit both SKF and SBAF, but blood-group reactive sugars cannot block either SKF or SBAF.

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The Nature of Secretory Agglutinins and Aggregating Factors

Cited by 8 publications

References 10 publications

Characterization of a Salivary Agglutinin Reacting with a Serotype c Strain of Streptococcus mutans

Characterization of a Salivary Agglutinin Reacting with a Serotype c Strain of Streptococcus mutans

Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage.

The Nature of Secretory Agglutinins and Aggregating Factors

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