Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious
            <i>Actinomyces</i>
            spp. Delineated by a Hybrid Peptide Construct

Niemi, Liza Danielsson; Johansson, Ingegerd

doi:10.1128/iai.72.2.782-787.2004

Cited by 13 publications

(15 citation statements)

References 27 publications

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“…In addition, the adhesion of P. gingivalis fimbriae (Amano et al, 1996a) and the cells of Actinomyces spp. (Niemi & Johansson, 2004) was not affected by statherin in solution. Domains of statherin involved in interaction with F. nucleatum are also thought to be cryptic.…”

Section: Discussionmentioning

confidence: 82%

“…2). Several reports have suggested that binding sites of salivary proteins including statherin and PRP1 in oral bacteria might be cryptic Amano et al, 1996a;Kataoka et al, 1997;Niemi & Johansson, 2004). PRP1, in solution, showed no inhibitory effect on adhesion of Streptococcus gordonii cells and P. gingivalis fimbriae (Kataoka et al, 1997) to PRP 1-coated HAP.…”

Section: Discussionmentioning

confidence: 99%

“…It inhibits primary and secondary precipitation of calcium salts; additionally, statherin is tightly adsorbed to enamel surfaces (Johnsson et al, 1993). Statherin promotes bacterial adhesion by organisms including Actinomyces viscosus (Gibbons et al, 1990;Niemi & Johansson, 2004), Actinomyces naeslundii (Strömberg et al, 1992;Niemi & Johansson, 2004) and Porphyromonas gingivalis (Amano et al, 1994) to surfaces such as hydroxyapatite (HAP) when it is pre-adsorbed to these surfaces. Xie et al (1991) demonstrated enhanced adsorption of F. nucleatum to statherin-coated hydroxyapatite (sHAP); however, the nature of statherin domain interaction with F. nucleatum remains unclear.…”

Section: Introductionmentioning

confidence: 99%

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Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells

et al. 2004

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Fusobacterium nucleatum can bind to saliva-coated tooth surfaces. However, the nature of the domains of salivary protein that interact with F. nucleatum remains unclear. The ability of individual proteins in human submandibular-sublingual saliva (HSMSL) to bind F. nucleatum cells was examined by dot blot assay; statherin displayed the strongest binding activity. Statherin binding sites were determined based on binding of 125 I-labelled F. nucleatum to statherin-coated hydroxyapatite (sHAP) beads via inhibition assays using synthetic analogous peptide fragments of whole statherin. Analogous peptides corresponding to residues 19-26 and 32-39 of statherin inhibited binding by 77 % and 68 %, respectively. Synthetic peptides were also prepared by serial deletions of individual residues from N-and C-termini of the peptides GPYQPVPE (aa 19-26) and QPYQPQYQ (aa 32-39). The inhibitory effects of peptides YQPVPE (aa 21-26) and PYQPQYQ (aa 33-39) were very similar to those of GPYQPVPE and QPYQPQYQ, respectively. However, additional deletion of residues resulted in significant reduction of the inhibitory effect. Alanine-scan analysis of YQPVPE revealed that all tested peptides retained inhibitory activity; only YAPVPE exhibited significantly decreased inhibitory activity. These findings suggest that YQPVPE and PYQPQYQ may represent the minimal active segments of statherin for binding to F. nucleatum; moreover, Gln may be a key amino acid in the active segment.

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Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells

et al. 2004

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“…It has a significant affinity for calcium phosphate precipitates, including hydroxyapatite, and is present as an enamel pellicle protein within the oral cavity (5). Statherin also contains sites for the adhesion of bacteria such as Porphyromonas gingivalis and Streptococcus mutans to the tooth surface (6,7), and these sites are thought to be a feature that the microorganisms have exploited for biofilm development (8). Therefore, it would be significant to determine whether FDC-SP has a similar activity to statherin.…”

Section: Fdc-spmentioning

confidence: 99%

Adsorption of Follicular Dendritic Cell-secreted Protein (FDC-SP) onto Mineral Deposits

Shinomura

Nakamura

et al. 2008

Journal of Biological Chemistry

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Follicular dendritic cell-secreted protein (FDC-SP) is a small secretory protein having structural similarities to statherin, a protein in saliva thought to play a role in calcium retention in saliva. In contrast, FDC-SP is thought to play a role in the immune system associated with germinal centers. We report here the very specific expression of FDC-SP in junctional epithelium at the gingival crevice. This region is very important for the host defense against pathogens and for periodontal protection. To be able to better understand the function of FDC-SP, we developed a novel gene expression system that exploited gene trapping and site-specific gene integration to introduce the protein into a mammalian cell culture system. Using this system we were able to express FDC-SP as a fusion protein with green fluorescent protein in an osteogenic progenitor cell line with long term stability, which we then used to find that the fusion protein specifically adsorbs onto mineral deposits and the surface of hydroxyapatite particles exogenously added to the culture. This adsorption was highly dependent on the structural integrity of FDC-SP. These results suggest that FDC-SP may play an important role, adsorbing onto the surface of cementum and alveolar bone adjacent to periodontal ligament and onto tooth surface at the gingival crevice. FDC-SP2 is a small secretory protein that was originally identified in primary follicular dendritic cells isolated from human tonsils (1) and was implicated in modulation of B cell activity (2). Recently, we have found that FDC-SP is expressed specifically in periodontal ligament and parotid gland and has molecular properties similar to those of statherin, a protein in saliva thought to function in preventing calcium precipitation (3).Both molecules are small in size (68 and 43 residues for mature human FDC-SP and statherin, respectively) and have a prolinerich region in their C-terminal half. In addition, these regions show a high degree of hydrophobicity in contrast to their N-terminal hydrophilic regions. Such structural similarities strongly suggested that additional roles for FDC-SP exist and that additional experiments looking for functional similarities between FDC-SP and statherin would be very informative.Statherin is a multifunctional molecule secreted from parotid and submandibular gland (4). It has a significant affinity for calcium phosphate precipitates, including hydroxyapatite, and is present as an enamel pellicle protein within the oral cavity (5). Statherin also contains sites for the adhesion of bacteria such as Porphyromonas gingivalis and Streptococcus mutans to the tooth surface (6, 7), and these sites are thought to be a feature that the microorganisms have exploited for biofilm development (8). Therefore, it would be significant to determine whether FDC-SP has a similar activity to statherin. However, a major obstacle in the functional analysis of FDC-SP is that only a small amount of protein can be obtained from tissues such as periodontal ligament and parotid gland. ...

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“…STATH plays a key role in the development of the oral cavity biofilm by mediating adhesion of bacteria and was recently identified as being the most prominent protein in the saliva-air interface (31). It is known to have bacterial binding epitopes that promote the growth and adhesion in the oral cavity of some organisms (Porphyromonas gingivalis and Fusobacterium nucleatum) while inhibiting the growth of others (Peptostreptococci and S. aureus) (14,32,33). Its antimicrobial effect on P. aeruginosa has not been investigated.…”

Section: Mild Versus Severe Cf Differential Gene Expressionmentioning

confidence: 99%

Respiratory Epithelial Gene Expression in Patients with Mild and Severe Cystic Fibrosis Lung Disease

Wright

Merlo

Reynolds

et al. 2006

Am J Respir Cell Mol Biol

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Despite having identical cystic fibrosis transmembrane conductance regulator genotypes, individuals with ⌬F508 homozygous cystic fibrosis (CF) demonstrate significant variability in severity of pulmonary disease. This investigation used high-density oligonucleotide microarray analysis of nasal respiratory epithelium to investigate the molecular basis of phenotypic differences in CF by (1 ) identifying differences in gene expression between ⌬F508 homozygotes in the most severe 20th percentile of lung disease by forced expiratory volume in 1 s and those in the most mild 20th percentile of lung disease and (2 ) identifying differences in gene expression between ⌬F508 homozygotes and age-matched non-CF control subjects. Microarray results from 23 participants (12 CF, 11 non-CF) met the strict quality control guidelines and were used for final data analysis. A total of 652 of the 11,867 genes identified as present in 75% of the samples were significantly differentially expressed in one of the three disease phenotypes: 30 in non-CF, 53 in mild CF, and 569 in severe CF. An analysis of genes differentially expressed by severity of CF lung disease demonstrated significant upregulation in severe CF of genes involved in protein ubiquination (P Ͻ 0.04), mitochondrial oxidoreductase activity (P Ͻ 0.01), and lipid metabolism (P Ͻ 0.03). Analysis of genes with decreased expression in patients with CF compared with control subjects demonstrated significant downregulation of genes involved in airway defense (P Ͻ 0.047) and protein metabolism (P Ͻ 0.048). This study suggests that differences in CF lung phenotype are associated with differences in expression of genes involving airway defense, protein ubiquination, and mitochondrial oxidoreductase activity and identifies specific new candidate modifiers of the CF phenotype.

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Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct

Cited by 13 publications

References 27 publications

Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells

Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells

Adsorption of Follicular Dendritic Cell-secreted Protein (FDC-SP) onto Mineral Deposits

Respiratory Epithelial Gene Expression in Patients with Mild and Severe Cystic Fibrosis Lung Disease

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