Sequence analyses of fimbriae subunit FimA proteins on Actinomyces naeslundii genospecies 1 and 2 and Actinomyces odontolyticus with variant carbohydrate binding specificities

BMC Microbiology

Volumn 6, Issue , 2006, Pages

  Drobni, Mirva ^a   Hallberg, Kristina ^a   Öhman, Ulla ^a   Birve, Anna ^a   Persson, Karina ^a   Johansson, Ingegerd ^a   Strömberg, Nicklas ^a  

^a UMEÅ UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

FIMBRIA PROTEIN; PILIN; PROTEIN FIM A; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

ACTINOMYCES NAESLUNDII; AMINO ACID SEQUENCE; ANTIGENICITY; ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; FIMBRIA; GENE SEQUENCE; HEMAGGLUTINATION; NONHUMAN; OLIGOMERIZATION; PROTEIN BINDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; WESTERN BLOTTING;

ACTINOMYCES; AMINO ACID SEQUENCE; ANTIBODIES, BACTERIAL; BLOTTING, WESTERN; CARBOHYDRATE METABOLISM; DNA, BACTERIAL; FIMBRIAE PROTEINS; GALACTOSAMINE; GALACTOSE; GENE ORDER; HEMAGGLUTINATION; MOLECULAR SEQUENCE DATA; N-ACETYLNEURAMINIC ACID; PHYLOGENY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECIES SPECIFICITY;

ACTINOMYCES; ACTINOMYCES NAESLUNDII; ACTINOMYCES ODONTOLYTICUS; POSIBACTERIA;

EID: 33744901679     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-6-43     Document Type: Article

References (39)

1. Hallberg K, Hammarström KJ, Falsen E, Dahlen G, Gibbons RJ, Hay DI, Strömberg N: Actinomyces naeslundii genospecies 1 and 2 express different binding specificities to N-acetyl-b-D-galactosamine, whereas Actinomyces odontolyticus expresses a different binding specificity in colonizing the human mouth. Oral Microbiol Immunol 1998, 13:327-336.
2. Johnson JL, Moore LV, Kaneko B, Moore WE: Actinomyces georgiae sp. nov., Actinomyces gerencseriae sp. nov., designation of two genospecies of Actinomyces naeslundii, and inclusion of A. naeslundii serotypes II and III and Actinomyces viscosus serotype II in A. naeslundii genospecies 2. Int J Syst Bacteriol 1990, 40:273-286.
3. Ellen RP: Establishment and distribution of Actinomyces viscosus and Actinomyces naeslundii in the human oral cavity. Infect Immun 1976, 14:1119-1124.
4. Mager DL, Ximenez-Fyvie LA, Haffajee AD, Socransky SS: Distribution of selected bacterial species on intraoral surfaces. J Clin Periodontol 2003, 30:644-654.
5. Nyvad B, Kilian M: Microflora associated with experimental root surface caries in humans. Infect Immun 1990, 58:1628-1633.
6. Becker MR, Paster BJ, Leys EJ, Moeschberger ML, Kenyon SG, Galvin JL, Boches SK, Dewhirst FE, Griffen AL: Molecular analysis of bacterial species associated with childhood caries. J Clin Microbiol 2002, 40:1001-1009.
7. Tanner A, Maiden MF, Macuch PJ, Murray LL, Kent RLJ: Microbiota of health, gingivitis, and initial periodontitis. J Clin Periodontol 1998, 25:85-98.
8. Raymond A, Smego J, Foglia G: Actinomycosis. Clinical Infectious Diseases 1998, 26:1255-1263.
9. Whittaker CJ, Klier CM, Kolenbrander PE: Mechanisms of adhesion by oral bacteria. Annu Rev Microbiol 1996, 50:513-552.
10. Gibbons RJ: Bacterial adhesion to oral tissues: a model for infectious diseases. J Dent Res 1989, 68:750-760.
11. Kolenbrander PE: Intergeneric coaggregation among human oral bacteria and ecology of dental plaque. Annu Rev Microbiol 1988, 42:627-656.
12. Cisar JO, Sandberg AL, Mergenhagen SE: The function and distribution of different fimbriae on strains of Actinomyces viscosus and Actinomyces naeslundii. J Dent Res 1984, 63:393-396.
13. Cisar JO, Vatter AE, Clark WB, Curl SH, Hurst Calderone S, Sandberg AL: Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae. Infect Immun 1988, 56:2984-2989.
14. Hallberg K, Holm C, Öhman U, Strömberg N: Actinomyces naeslundii displays variant fimP and fimA fimbrial subunit genes corresponding to different types of acidic proline-rich protein and beta-linked galactosamine binding specificity. Infect Immun 1998, 66:4403-4410.
15. Gibbons RJ, Hay DI: Human salivary acidic proline-rich proteins and statherin promote the attachment of Actinomyces viscosus LY7 to apatitic surfaces. Infect Immun 1988, 56:439-445.
16. Stromberg N, Karlsson KA: Characterization of the binding of Actinomyces naeslundii (ATCC 12104) and Actinomyces viscosus (ATCC 19246) to glycosphingolipids, using a solidphase overlay approach. J Biol Chem 1990, 265:11251-11258.
17. Stromberg N, Boren T, Carlen A, Olsson J: Salivary receptors for GalNAc beta-sensitive adherence of Actinomyces spp.: evidence for heterogeneous GalNAc beta and proline-rich protein receptor properties. Infect Immun 1992, 60:3278-3286.
18. Cisar JO, Sandberg AL, Reddy GP, Abeygunawardana C, Bush CA: Structural and antigenic types of cell wall polysaccharides from viridans group streptococci with receptors for oral actinomyces and streptococcal lectins. Infect Immun 1997, 65:5035-5041.
19. Brennan MJ, Cisar JO, Vatter AE, Sandberg AL: Lectin-dependent attachment of Actinomyces naeslundii to receptors on epithelial cells. Infect Immun 1984, 46:459-464.
20. Strömberg N, Borén T: Actinomyces tissue specificity may depend on differences in receptor specificity for GalNAc beta-containing glycoconjugates. Infect Immun 1992, 60:3268-3277.
21. Sandberg AL, Ruhl S, Joralmon RA, Brennan MJ, Sutphin MJ, Cisar JO: Putative glycoprotein and glycolipid polymorphonuclear leukocyte receptors for the Actinomyces naeslundii WVU45 fimbrial lectin. Infect Immun 1995, 63:2625-2631.
22. Yeung MK: Conservation of an Actinomyces viscosus T14V type 1 fimbrial subunit homolog among divergent groups of Actinomyces spp. Infect Immun 1992, 60:1047-1054.
23. Yeung MK, Chassy BM, Cisar JO: Cloning and expression of a type 1 fimbrial subunit of Actinomyces viscosus T14V. J Bacteriol 1987, 169:1678-1683.
24. Yeung MK, Cisar JO: Cloning and nucleotide sequence of a gene for Actinomyces naeslundii WVU45 type 2 fimbriae. J Bacteriol 1988, 170:3803-3809.
25. Yeung MK, Cisar JO: Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp. J Bacteriol 1990, 172:2462-2468.
26. Yeung MK, Ragsdale PA: Synthesis and function of Actinomyces naeslundii T14V type 1 fimbriae require the expression of additional fimbria-associated genes. Infect Immun 1997, 65:2629-2639.
27. Li T, Khah MK, Slavnic S, Johansson I, Strömberg N: Different type 1 fimbrial genes and tropisms of commensal and potentially pathogenic Actinomyces spp. with different salivary acidic proline-rich protein and statherin ligand specificities. Infect Immun 2001, 69:7224-7233.
28. Loimaranta V, Jakubovics NS, Hytonen J, Finne J, Jenkinson HF, Strömberg N: Fluid- or surface-phase human salivary scavenger protein gp340 exposes different bacterial recognition properties. Infect Immun 2005, 73:2245-2252.
29. Ton-That H, Marraffini LA, Schneewind O: Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae. Mol Microbiol 2004, 53:251-261.
30. Ton-That H, Schneewind O: Assembly of pili on the surface of Corynebacterium diphtheriae. Mol Microbiol 2003, 50:1429-1438.
31. Ton-That H, Marraffini LA, Schneewind O: Protein sorting to the cell wall envelope of Gram-positive bacteria. Biochim Biophys Acta 2004, 1694:269-278.
32. van Die I, Hoekstra W, Bergmans H: Analysis of the primary structure of P-fimbrillins of uropathogenic Escherichia coli. Microb Pathog 1987, 3:149-154.
33. Yeung MK: Complete nucleotide sequence of the Actinomyces viscosus T14V sialidase gene: presence of a conserved repeating sequence among strains of Actinomyces spp. Infect Immun 1993, 61:109-116.
34. Molecular Toolkit [http://arbl.cvmbs.colostate.edu/molkit/index.html]. .
35. Genome Net, ClustalW [http://clustalw.genome.jp/]. .
36. Center for Biological Sequence analysis, SignalP server [http://www.cbs.dtu.dk/services/SignalP/]. .
37. ExPASy Proteomics Server, ScanProsite [http://www.expasy.org/tools/ scanprosite/]. .
38. My hits, motif scan [http://myhits.isb-sib.ch/cgi-bin/motif_scan]. .
39. Navarre WW, Schneewind O: Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol Microbiol 1994, 14:115-121.