Pellicle receptors for Actinomyces viscosus type 1 fimbriae in vitro

Clark, William; Beem, J E; Nesbitt, W E; Cisar, John O.; Tseng, Chien‐Chi; Levine, Michael

doi:10.1128/iai.57.10.3003-3008.1989

Cited by 62 publications

(31 citation statements)

References 31 publications

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“…Basic proline-rich proteins comprise approximately 23% of saliva proteins and bind oral bacteria, e.g. A. viscous (Clark et al, 1989), F. nucleatum (Gillece-Castro et al, 1991), and S. gordonii (Ligtenberg et al, 1992) as well as hydroxyapatite. Furthermore, the surface of various oral bacterial strains such as Gemella haemolysans, Gemella morbillorium, Streptococcus acidominimus, Streptococcus oralis, Streptococcus salivarius, and Streptococcus parasanguinis binds to salivary PIPs (Schenkels et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Alpha‐amylase is a human salivary protein with affinity to lipopolysaccharide of Aggregatibacter actinomycetemcomitans

Baik

Hong

Choi

et al. 2012

Molecular Oral Microbiology

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Aggregatibacter actinomycetemcomitans lipopolysaccharide (Aa.LPS) is a major virulence factor associated with aggressive periodontitis. Although the recognition of Aa.LPS is potentially initiated by salivary proteins in the oral cavity, Aa.LPS-binding proteins (Aa.LPS-BPs) in saliva are poorly characterized. The purpose of this study was to capture and identify Aa.LPS-BPs in human saliva using a LTQ-Orbitrap hybrid Fourier transform mass spectrometry. Aa.LPS conjugated onto N-hydroxysuccinimidyl-Sepharose(®) 4 Fast Flow beads (Aa.LPS-beads) activated Toll-like receptor 4 and produced nitric oxide and Interferon gamma-inducible protein-10, implying that the conjugation process did not alter the biological properties of Aa.LPS. Aa.LPS-BPs were subsequently isolated from the nine human saliva samples from healthy individuals with the Aa.LPS-beads followed by identification with the mass spectrometry. Aa.LPS-BPs include α-amylase, serum albumin, cystatin, lysozyme C, submaxillary gland androgen-regulated protein 3B, immunoglobulin subunits, polymeric immunoglobulin receptor, deleted in malignant brain tumors 1, prolactin-inducible protein, lipocalin-1, and basic salivary proline-rich protein 2. Specific binding was validated using a pull-down assay with α-amylase which was captured at the highest frequency. Alpha-amylase demonstrated to interfere with the adherence and biofilm formation of A. actinomycetemcomitans. Even heat-inactivated α-amylase showed the interference to the same extent. Conclusively, we identified unique Aa.LPS-BPs that provide useful information to understand bacterial pathogenesis and host innate immunity in the oral cavity.

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Section: Discussionmentioning

confidence: 99%

Alpha‐amylase is a human salivary protein with affinity to lipopolysaccharide of Aggregatibacter actinomycetemcomitans

Baik

Hong

Choi

et al. 2012

Molecular Oral Microbiology

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“…The early-colonizing bacteria are primarily represented by Gram-positive species which have the ability to adhere directly to the salivary pellicle and the tooth surface. Examples of early colonizers include streptococci and actinomyces, which possess surface components such as fimbriae and receptor polysaccharides that mediate inter-and intrageneric co-aggregation and allow for attachment to salivary proteins and the tooth surface (Clark et al, 1989;Palmer et al, 2003;Ruhl et al, 2004). Late-colonizing bacteria are represented by a variety of Gram-negative bacteria including the periodontal pathogens Aggregatibacter actinomycetemcomitans, Treponema denticola and Porphyromonas gingivalis.…”

Section: Introductionmentioning

confidence: 99%

The Fusobacterium nucleatum outer membrane protein RadD is an arginine‐inhibitable adhesin required for inter‐species adherence and the structured architecture of multispecies biofilm

Kaplan¹,

Lux²,

Haake³

et al. 2008

Molecular Microbiology

196

247

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SummaryA defining characteristic of the suspected periodontal pathogen Fusobacterium nucleatum is its ability to adhere to a plethora of oral bacteria. This distinguishing feature is suggested to play an important role in oral biofilm formation and pathogenesis, with fusobacteria proposed to serve as central "bridging organisms" in the architecture of the oral biofilm bringing together species which would not interact otherwise. Previous studies indicate that these bacterial interactions are mediated by galactose-or arginine-inhibitable adhesins although genetic evidence for the role and nature of these proposed adhesins remains elusive. To characterize these adhesins at the molecular level, the genetically transformable F. nucleatum strain ATCC 23726 was screened for adherence properties, and arginine inhibitable adhesion was evident, while galactose-inhibitable adhesion was not detected. Six potential arginine binding proteins were isolated from the membrane fraction of F. nucleatum ATCC 23726 and identified via mass spectroscopy as members of the outer membrane family of proteins in F. nucleatum. Inactivation of the genes encoding these six candidates for arginineinhibitable adhesion and two additional homologues revealed that only a mutant derivative carrying an insertion in Fn1526 (now designated as radD) demonstrated significantly decreased coaggregation with representatives of the Gram-positive "early oral colonizers". Lack of the 350 kDa outer membrane protein encoded by radD resulted in the failure to form the extensive structured biofilm observed with the parent strain when grown in the presence of Streptococcus sanguinis ATCC 10556. These findings indicate that radD is responsible for arginine-inhibitable adherence of F. nucleatum and provides definitive molecular evidence that F. nucleatum adhesins play a vital role in inter-species adherence and multispecies biofilm formation.

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“…Adhesins on the surface of oral bacterial cells are necessary for initial colonization and enable these cells to attach to the salivary pellicle (6). In addition, Actinomyces species exhibit coaggregation reactions with a variety of different bacteria (5,15,26,28).…”

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confidence: 99%

Coaggregation of Candida albicans oral Actinomyces species

Grimaudo

Nesbitt

Clark

1996

Oral Microbiology and Immunology

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Eight strains of Actinomyces were examined for their ability to coaggregate in vitro with four strains of Candida albicans. The Actinomyces coaggregated to various degrees with all of the Candida strains. Exposure of the Candida but not the Actinomyces to heat, trypsin, proteinase K, amphotericin B or trichodermin abolished coaggregation. All sugars tested did not inhibit any of the reactions. All coaggregating pairs were disaggregated by the addition of SDS, but nonionic detergents had no effect. The addition of urea or EDTA completely reversed coaggregation. Actinomyces strains were sensitive to periodate oxidation, whereas the Candida strains were unaffected. These data suggest that the coaggregations involve a protein on the Candida surface that may interact with carbohydrates or carbohydrate-containing molecules on the surface of the Actinomyces. These observations expand the known range of intergeneric coaggregations occurring between human oral microbes and indicate that coaggregation of C. albicans and Actinomyces may be an important factor in oral colonization by this yeast.

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Pellicle receptors for Actinomyces viscosus type 1 fimbriae in vitro

Cited by 62 publications

References 31 publications

Alpha‐amylase is a human salivary protein with affinity to lipopolysaccharide of Aggregatibacter actinomycetemcomitans

Alpha‐amylase is a human salivary protein with affinity to lipopolysaccharide of Aggregatibacter actinomycetemcomitans

The Fusobacterium nucleatum outer membrane protein RadD is an arginine‐inhibitable adhesin required for inter‐species adherence and the structured architecture of multispecies biofilm

Coaggregation of Candida albicans oral Actinomyces species

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