Characterization of a Galactose-Specific Lectin from
            <i>Actinomyces viscosus</i>
            by a Model Aggregation System

Heeb, Mary J.; Costello, Ann; Gabriel, Othmar

doi:10.1128/iai.38.3.993-1002.1982

Cited by 26 publications

(19 citation statements)

References 35 publications

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“…The phenomenon of coaggregation between oral bacteria has been shown by a number of investigators to involve cell surface receptors (2,3,6,11). We chose to investigate bacteriophages as a potential tool for studying the structural components involved in coaggregations.…”

Section: Discussionmentioning

confidence: 99%

Simultaneous loss of bacteriophage receptor and coaggregation mediator activities in Actinomyces viscosus MG-1

Tylenda¹,

Enriquez²,

Kolenbrander³

et al. 1985

Infect Immun

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Actinomyces bacteriophages were used as tools to study coaggregation between actinomyces and streptococci. Four bacteriophage isolates, phages AV-1, AV-2, AV-3, and 1281, bound to coaggregation group A Actinomyces viscosus and to group E A. naeslundii. No binding to groups B, C, D, or F was observed. Only A. viscosus MG-1 was capable of supporting a productive infection by these phages. Spontaneously occurring bacteriophage-resistant mutants of A. viscosus MG-1 were isolated and were shown to fall into two classes. Class I mutants were resistant to all four phages, whereas class II mutants were resistant only to phage AV-3. In each case, strains resistant to a particular phage were unable to bind that phage, suggesting that a loss or alteration of the cell surface phage receptor had occurred. Both classes of mutants were unable to coaggregate with streptococci representing coaggregation group 1 and had also lost the ability to mediate one type of coaggregation with group 4 streptococci. Class II mutants also were unable to coaggregate with group 2 streptococci. Lactose-inhibitable interactions with other streptococci (groups 3 and 4) were unchanged in the mutants. The simultaneous loss of sensitivity to phage AV-3 and the ability to coaggregate with coaggregation group 1 streptococci suggests the possibility of a relationship between these two cell surface structures.were tested for the presence of phage as described previ-228 on August 9, 2020 by guest http://iai.asm.org/ Downloaded from

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Section: Discussionmentioning

confidence: 99%

Simultaneous loss of bacteriophage receptor and coaggregation mediator activities in Actinomyces viscosus MG-1

Tylenda¹,

Enriquez²,

Kolenbrander³

et al. 1985

Infect Immun

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“…These findings may reflect subtle differences in the affinity and fine specificity of the lectin combining sites (25) or in the regulation of fimbria-tion by environmental factors. Since the unmasking of receptors on mammalian cells by neuraminidase significantly enhances bacterial adherence (1,10,16,21,33), the production of this enzyme by bacteria and the susceptibility of various mammalian cells to neuraminidase represent other variables that could influence binding of the fimbrial lectin to different tissue surfatces. Thus, further studies may well reveal additional molecular determinants that influence the in vivo distribution of A. naeslundii, A. viscosus, and other oral bacteria.…”

Section: Discussionmentioning

confidence: 99%

Exclusive presence of lactose-sensitive fimbriae on a typical strain (WVU45) of Actinomyces naeslundii

Cisar¹,

David²,

Curl³

et al. 1984

Infect Immun

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Lactose-sensitive fimbriae were identified as the only fimbriae present on Actinomyces naeslundii WVU45 (ATCC 12104). A single antigen reactive with antiserum against WVU45 cells was detected by cross immunoelectrophoresis of isolated fimbriae, and a monospecific antiserum against this antigen reacted with all fimbriae observed on the bacterial surface by immunoelectron microscopy. Moreover, the loss of one cell surface antigen by a spontaneous mutant of A. naeslundii WVU45 (WVU45M), isolated by its failure to react with a monospecific antibody against the fimbriae, was associated with the loss of all fimbriae. The functional involvement of the fimbriae in lactose-sensitive bacterial adherence was demonstrated by the ability of WVU45, but not WVU45M, cells to agglutinate neuraminidase-treated erythrocytes and by the lactose-sensitive hemagglutinating activity of immune complexes formed with isolated fimbriae and monospecific antibody. Bacterial agglutination assays with different monospecific antibodies revealed an antigenic similarity between the fimbriae of A. naeslundii WVU45 and the lactose-sensitive fimbriae (type 2) of Actinomyces viscosus T14V. In contrast, cross-reactivity was not observed between the WVU45 fimbriae and type 1 fimbriae, the structures involved in lactose-resistant adherence of strain T14V to saliva-treated hydroxyapatite. Functional differences between the fimbriae of A. naeslundii and A. viscosus strains may be correlated with well-established differences in the in vivo distribution of these organisms: namely, the preference of typical A. naeslundii for epithelial surfaces and of A. viscosus for tooth surfaces.

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“…Lectins-carbohydrate-targeting proteins via specific sugar recognition-are a good example of adhesins that are synthesized by the cells for this purpose. Interestingly, lectins are often located on the tip or in the subunit of fimbriae or pili, rendering these appendages more mechanistically powerful in bacterial adhesion (Heeb et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Characterization of Lectins and Bacterial Adhesins in Activated Sludge Flocs

Park

Novak

2009

Water Environment Research

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Bacterial lectins are carbohydrate‐binding proteins that are involved in bacterial adhesion and aggregation. To investigate whether lectins are involved in floc formation of activated sludge, hemaaggultination (HA) and HA inhibition assays were conducted on extracellular polymeric substances (EPS) extracted from activated sludges. Six sludges from both full‐scale and synthetic chemical‐fed laboratory activated sludge systems were subjected to EPS extraction and lectin assay. Activated sludge EPS resulted in strong agglutination with trypsin‐treated human red blood cells. While simple monosaccharides failed to exhibit inhibition of agglutination, several glycoproteins clearly reversed agglutination, indicating that glycoprotein (oligosaccharide)‐specific lectins are present in activated sludge. This inhibitory pattern was the same for both the field and laboratory‐grown activated sludges, indicating that these lectins are indigenously generated by activated sludge microorganisms. The major lectin activities were found to be present in a hydrophobic region of EPS. The activities remained unaffected after heat and urea treatment of EPS, but were significantly reduced by the ethylenediaminetetraacetic acid (EDTA) treatment. These results share similar properties with previously studied pure culture bacterial lectins and support the conclusion that lectin‐mediated bacterial aggregation is one of the mechanisms responsible for activated sludge bioflocculation.

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Characterization of a Galactose-Specific Lectin from Actinomyces viscosus by a Model Aggregation System

Cited by 26 publications

References 35 publications

Simultaneous loss of bacteriophage receptor and coaggregation mediator activities in Actinomyces viscosus MG-1

Simultaneous loss of bacteriophage receptor and coaggregation mediator activities in Actinomyces viscosus MG-1

Exclusive presence of lactose-sensitive fimbriae on a typical strain (WVU45) of Actinomyces naeslundii

Characterization of Lectins and Bacterial Adhesins in Activated Sludge Flocs

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