Structural preferences of beta-galactoside-reactive lectins on Actinomyces viscosus T14V and Actinomyces naeslundii WVU45

McIntire, Floyd C.; Crosby, L K; Barlow, Joseph J.; Matta, Khushi L.

doi:10.1128/iai.41.2.848-850.1983

Cited by 44 publications

(27 citation statements)

References 8 publications

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“…data). The present findings support the proposal (Drobni et al, 2006) that differences in the structural specificity of type 2 fimbriaemediated adhesion between strains of A. oris and A. naeslundii (McIntire et al, 1983;Stromberg and Karlsson, Fig . 7.…”

Section: Fig 6 Role Of Actinomyces Fima In Biofilm Formation Wild-supporting

confidence: 92%

The Actinomyces oris type 2 fimbrial shaft FimA mediates co‐aggregation with oral streptococci, adherence to red blood cells and biofilm development

Mishra

Yang

et al. 2010

Molecular Microbiology

122

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Interbacterial interactions between oral streptococci and actinomyces and their adherence to tooth surface and the associated host cells are key early events that promote development of the complex oral biofilm referred to as dental plaque. These interactions depend largely on a lectin-like activity associated with the Actinomyces oris type 2 fimbria, a surface structure assembled by sortase (SrtC2)-dependent polymerization of the shaft and tip fimbrillins, FimA and FimB, respectively. To dissect the function of specific fimbrillins in various adherence processes, we have developed a convenient new technology for generating unmarked deletion mutants of A. oris. Here, we show that the fimB mutant, which produced type 2 fimbriae composed only of FimA, like the wild type coaggregated strongly with receptor-bearing streptococci, agglutinated with sialidase-treated RBC, and formed monospecies biofilm. In contrast, the fimA and srtC2 mutants lacked type 2 fimbriae and were non-adherent in each of these assays. Plasmidbased expression of the deleted gene in respective mutants restored adherence to wild-type levels. These findings uncover the importance of the lectin-like activity of the polymeric FimA shaft rather than the tip. The multivalent adhesive function of FimA makes it an ideal molecule for exploring novel intervention strategies to control plaque biofilm formation.

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Section: Fig 6 Role Of Actinomyces Fima In Biofilm Formation Wild-supporting

confidence: 92%

The Actinomyces oris type 2 fimbrial shaft FimA mediates co‐aggregation with oral streptococci, adherence to red blood cells and biofilm development

Mishra

Yang

et al. 2010

Molecular Microbiology

122

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“…Thus, it is of interest that typical A. naeslundii inhabits epithelial surfaces and is abundant in saliva and that, whereas it can be found in dental plaque, it is not among the organisms regarded as primary colonizers of the tooth surface (34). These observations favor a role for the fimbrial lectin in bacterial adherence to epithelial cells (1,17,32,33) and to specific plaque bacteria such as strains of Streptococcus sanguis (6,15,(25)(26)(27). They also suggest that lactosesensitive adherence may not be a mechanism of primary importance in the adsorption of bacteria to the acquired pellicle of teeth.…”

Section: Discussionmentioning

confidence: 99%

“…This possibility is suggested by differences between A. viscosus and A. naeslundii strains in their lactose-sensitive coaggregations with specific streptococci (6) and also by obvious differences in the extent to which certain Actinomyces strains cause agglutination of neuraminidase-treated erythrocytes (10, 16). 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.…”

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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“…The genospecies 2 strains LY7 and ATCC 19246, both expressing type 1 fimbriae (16,47) and isolated from human sites, display preferential binding to APRPs and statherin, respectively (40,41). Type 2 fimbriae, expressed by both genospecies (8,39), mediate binding to ␤1-3-linked galactose or galactosamine structures (referred to as GalNAc␤ specificity) (33,43) in cell surface glycolipids and glycoproteins (5,40), salivary glycoproteins (41), and streptococcal capsular polysaccharides (1). However, the genospecies 1 strain ATCC 12104 T and the genospecies 2 strain LY7 display different binding patterns to a panel of saccharides containing ␤-linked galactose or galactosamine structures (39,40).…”

mentioning

confidence: 99%

Actinomyces naeslundii Displays Variant fimP and fimA Fimbrial Subunit Genes Corresponding to Different Types of Acidic Proline-Rich Protein and β-Linked Galactosamine Binding Specificity

et al. 1998

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Actinomyces naeslundii genospecies 1 and 2 bind to acidic proline-rich proteins (APRPs) and statherin via type 1 fimbriae and to ␤-linked galactosamine (GalNAc␤) structures via type 2 fimbriae. In addition, A. naeslundii displays two types of binding specificity for both APRPs-statherin and GalNAc␤, while Actinomyces odontolyticus binds to unknown structures. To study the molecular basis for these binding specificities, DNA fragments spanning the entire or central portions of fimP (type 1) and fimA (type 2) fimbrial subunit genes were amplified by PCR from strains of genospecies 1 and 2 and hybridized with DNA from two independent collections of oral Actinomyces isolates. Isolates of genospecies 1 and 2 and A. odontolyticus, but no other Actinomyces species, were positive for hybridization with fimP and fimA full-length probes irrespective of binding to APRPs and statherin, GalNAc␤, or unknown structures. Isolates of genospecies 1 and 2, with deviating patterns of GalNAc␤1-3Gal␣-O-ethyl-inhibitable coaggregation with Streptococcus oralis Ss34 and MPB1, were distinguished by a fimA central probe from genospecies 1 and 2, respectively. Furthermore, isolates of genospecies 1 and 2 displaying preferential binding to APRPs over statherin were positive with a fimP central probe, while a genospecies 2 strain with the opposite binding preference was not. The sequences of fimP and fimA central gene segments were highly conserved among isolates with the same, but diversified between those with a variant, binding specificity. In conclusion, A. naeslundii exhibits variant fimP and fimA genes corresponding to diverse APRP and GalNAc␤ specificities, respectively, while A. odontolyticus has a genetically related but distinct adhesin binding specificity.

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Structural preferences of beta-galactoside-reactive lectins on Actinomyces viscosus T14V and Actinomyces naeslundii WVU45

Cited by 44 publications

References 8 publications

The Actinomyces oris type 2 fimbrial shaft FimA mediates co‐aggregation with oral streptococci, adherence to red blood cells and biofilm development

The Actinomyces oris type 2 fimbrial shaft FimA mediates co‐aggregation with oral streptococci, adherence to red blood cells and biofilm development

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

Actinomyces naeslundii Displays Variant fimP and fimA Fimbrial Subunit Genes Corresponding to Different Types of Acidic Proline-Rich Protein and β-Linked Galactosamine Binding Specificity

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