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

Hallberg, K.; Holm, Charlotta; Öhman, Ulla; Strömberg, Nicklas

doi:10.1128/iai.66.9.4403-4410.1998

Cited by 27 publications

(29 citation statements)

References 48 publications

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“…The adherence of actinomycetes to eukaryotic host cells and other bacteria, including several streptococcal species, is directed by a separate set of fimbriae designated type 2. Type 2 fimbriae appear to utilize a lectin-like activity to bind to the surface of target cells, and this binding can often be disrupted by high concentrations of sugars such as lactose (298,440).…”

Section: Fimbriae Of Actinomycesmentioning

confidence: 99%

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Navarre

Schneewind

1999

Microbiol Mol Biol Rev

1,185

601

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SUMMARY The cell wall envelope of gram-positive bacteria is a macromolecular, exoskeletal organelle that is assembled and turned over at designated sites. The cell wall also functions as a surface organelle that allows gram-positive pathogens to interact with their environment, in particular the tissues of the infected host. All of these functions require that surface proteins and enzymes be properly targeted to the cell wall envelope. Two basic mechanisms, cell wall sorting and targeting, have been identified. Cell well sorting is the covalent attachment of surface proteins to the peptidoglycan via a C-terminal sorting signal that contains a consensus LPXTG sequence. More than 100 proteins that possess cell wall-sorting signals, including the M proteins of Streptococcus pyogenes, protein A of Staphylococcus aureus, and several internalins of Listeria monocytogenes, have been identified. Cell wall targeting involves the noncovalent attachment of proteins to the cell surface via specialized binding domains. Several of these wall-binding domains appear to interact with secondary wall polymers that are associated with the peptidoglycan, for example teichoic acids and polysaccharides. Proteins that are targeted to the cell surface include muralytic enzymes such as autolysins, lysostaphin, and phage lytic enzymes. Other examples for targeted proteins are the surface S-layer proteins of bacilli and clostridia, as well as virulence factors required for the pathogenesis of L. monocytogenes (internalin B) and Streptococcus pneumoniae (PspA) infections. In this review we describe the mechanisms for both sorting and targeting of proteins to the envelope of gram-positive bacteria and review the functions of known surface proteins.

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Section: Fimbriae Of Actinomycesmentioning

confidence: 99%

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Navarre

Schneewind

1999

Microbiol Mol Biol Rev

1,185

601

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“…Thus, strains of A. naeslundii genospecies 1 and 2 from the human mouth show preferential binding to APRPs over statherin (18), while A. viscosus ATCC 19246, originating from a human with cervicofacial actinomycosis, displays preferential binding to statherin (51). DNA-DNA hybridization with specific fimP probes shows a genetic diversity among fimP genes encoding type 1 fimbriae (20,49). Recently, recombinant P. gingivalis fimbrillin, which binds to statherin and to APRPs, was found to interact with Leu 29 Tyr 30 and Tyr 41 Thr 42 Phe 43 of statherin (1).…”

mentioning

confidence: 97%

“…The binding sites for A. naeslundii LY7 (45) and Streptococcus gordonii Blackburn (16) reside in the Pro 149 Gln 150 carboxy termini of APRPs. The patterns of binding to APRPs and statherin differ among bacterial species and individual strains of A. naeslundii (20,49,51). Thus, strains of A. naeslundii genospecies 1 and 2 from the human mouth show preferential binding to APRPs over statherin (18), while A. viscosus ATCC 19246, originating from a human with cervicofacial actinomycosis, displays preferential binding to statherin (51).…”

mentioning

confidence: 98%

“…Actinomyces naeslundii and Actinomyces viscosus form considerable portions of the microflora on oral surfaces in humans and in animal species like the rat and hamster, respectively. Adhesion of A. naeslundii (A. naeslundii genospecies 1 and 2 and A. viscosus serotype II, according to current taxonomy [28]) involves two distinct fimbriae, type 1 and type 2, while less is known about adhesive properties in A. viscosus (A. viscosus serotype I [28]) (6,7,20,49). Type 1 fimbriae promote a protein-protein interaction with tooth-adsorbed salivary acidic proline-rich proteins (APRPs) and statherin (13,15), while type 2 fimbriae bind to ␤-linked galactose and galactosamine structures on epithelial and bacterial cell surfaces (18,34,52,56).…”

mentioning

confidence: 99%

“…Type 1 fimbriae are consequently thought to participate in early plaque development, and type 2 fimbriae are thought to participate in late plaque development and colonization of the oral mucosa (6,7,12,18,49,50,56). Thus, expression of type 1 and type 2 fimbriae and their variant binding types (20,49) enables A. naeslundii to establish distinct intraoral colonization niches (6,11,18).…”

mentioning

confidence: 99%

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Strains of Actinomyces naeslundii and Actinomyces viscosus Exhibit Structurally Variant Fimbrial Subunit Proteins and Bind to Different Peptide Motifs in Salivary Proteins

Johansson

Hay

et al. 1999

Infect Immun

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Oral strains of Actinomyces spp. express type 1 fimbriae, which are composed of major FimP subunits, and bind preferentially to salivary acidic proline-rich proteins (APRPs) or to statherin. We have mapped genetic differences in the fimPsubunit genes and the peptide recognition motifs within the host proteins associated with these differential binding specificities. ThefimP genes were amplified by PCR from Actinomyces viscosus ATCC 19246, with preferential binding to statherin, and from Actinomyces naeslundii LY7, P-1-K, and B-1-K, with preferential binding to APRPs. The fimP gene from the statherin-binding strain 19246 is novel and has about 80% nucleotide and amino acid sequence identity to the highly conservedfimP genes of the APRP-binding strains (about 98 to 99% sequence identity). The novel FimP protein contains an amino-terminal signal peptide, randomly distributed single-amino-acid substitutions, and structurally different segments and ends with a cell wall-anchoring and a membrane-spanning region. When agarose beads with CNBr-linked host determinant-specific decapeptides were used, A. viscosus 19246 bound to the Thr42Phe43terminus of statherin and A. naeslundii LY7 bound to the Pro149Gln150 termini of APRPs. Furthermore, while the APRP-binding A. naeslundii strains originate from the human mouth, A. viscosus strains isolated from the oral cavity of rat and hamster hosts showed preferential binding to statherin and contained the novel fimP gene. Thus, A. viscosus and A. naeslundii display structurally variant fimP genes whose protein products are likely to interact with different peptide motifs and to determine animal host tropism.

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Actinomyces

Schaal¹,

Yassin²

2015

Bergey's Manual of Systematics of Archaea and Bacteria

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Ac.ti.no.my'ces. Gr. fem. n. aktis, aktinos ray; Gr. masc. n. mukês fungus; N.L. masc. n. Actinomyces ray fungus referring to the radial arrangement of filaments in Actinomyces bovis sulfur granules. Actinobacteria / Actinobacteria / Actinomycetales / Actinomycetaceae / Actinomyces Straight or slightly curved rods , 0.2–1.0 µm in diameter, which vary considerably in shape and size, and slender filaments , 1 µm or less in width and 10–50 µm or more in length, with true branching. Short rods (0.5–5.0 µm in length) with or without clubbed ends are frequently seen and may occur singly, in pairs with diphtheroidal arrangements (Y, V, T forms and palisades), in short chains or in small clusters. Longer (5.0–10.0 µm in length) branched rods are also common. Several members of the genus appear chiefly or exclusively as coccobacillary or even coccoid elements. Filaments which may predominate in certain species are either straight or wavy , show varying degrees of branching and may have swollen, clubbed, or clavate ends. Gram‐stain‐positive , but irregular staining giving rise to a beaded or barred appearance frequently occurs, and two species may be Gram‐stain‐variable. Non‐acid‐fast, nonmotile, and non‐endospore‐forming. Conidia are not produced. DNA G+C content (mol%) : 55–71 ( T m , HPLC). Type species : Actinomyces bovis Harz 1877, 133 AL .

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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

Cited by 27 publications

References 48 publications

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope

Strains of Actinomyces naeslundii and Actinomyces viscosus Exhibit Structurally Variant Fimbrial Subunit Proteins and Bind to Different Peptide Motifs in Salivary Proteins

Actinomyces

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