Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1993 Jan;175(2):572–574. doi: 10.1128/jb.175.2.572-574.1993

Saliva-binding protein (SsaB) from Streptococcus sanguis 12 is a lipoprotein.

N Ganeshkumar 1, N Arora 1, P E Kolenbrander 1
PMCID: PMC196177  PMID: 8419308

Abstract

Two lipoprotein consensus sequences (Leu-X-X-Cys) are found in the presumptive signal peptide region (positions 12 to 15 and 17 to 20) of saliva-binding protein (SsaB) from Streptococcus sanguis 12. Three analogs of SsaB containing Cys-->Gly mutations were constructed by site-directed mutagenesis of pSA2, the recombinant plasmid expressing SsaB. [3H]palmitate was incorporated into SsaB only when the native Cys-20 residue was present. These data show that SsaB is a lipoprotein and that Cys-20 is the critical site for acylation.

Full text

PDF
572

Images in this article

573Image
on p.573
573Image
on p.573
574Image
on p.574

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arora N., Klimpel K. R., Singh Y., Leppla S. H. Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells. J Biol Chem. 1992 Aug 5;267(22):15542–15548. [PubMed] [Google Scholar]
  2. Clark W. B., Bammann L. L., Gibbons R. J. Comparative estimates of bacterial affinities and adsorption sites on hydroxyapatite surfaces. Infect Immun. 1978 Mar;19(3):846–853. doi: 10.1128/iai.19.3.846-853.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Demuth D. R., Golub E. E., Malamud D. Streptococcal-host interactions. Structural and functional analysis of a Streptococcus sanguis receptor for a human salivary glycoprotein. J Biol Chem. 1990 May 5;265(13):7120–7126. [PubMed] [Google Scholar]
  4. Fachon-Kalweit S., Elder B. L., Fives-Taylor P. Antibodies that bind to fimbriae block adhesion of Streptococcus sanguis to saliva-coated hydroxyapatite. Infect Immun. 1985 Jun;48(3):617–624. doi: 10.1128/iai.48.3.617-624.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fenno J. C., LeBlanc D. J., Fives-Taylor P. Nucleotide sequence analysis of a type 1 fimbrial gene of Streptococcus sanguis FW213. Infect Immun. 1989 Nov;57(11):3527–3533. doi: 10.1128/iai.57.11.3527-3533.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ganeshkumar N., Hannam P. M., Kolenbrander P. E., McBride B. C. Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB) from Streptococcus sanguis 12 and possible role of the protein in coaggregation with actinomyces. Infect Immun. 1991 Mar;59(3):1093–1099. doi: 10.1128/iai.59.3.1093-1099.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ganeshkumar N., Song M., McBride B. C. Cloning of a Streptococcus sanguis adhesin which mediates binding to saliva-coated hydroxyapatite. Infect Immun. 1988 May;56(5):1150–1157. doi: 10.1128/iai.56.5.1150-1157.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gibbons R. J., Hay D. I., Schlesinger D. H. Delineation of a segment of adsorbed salivary acidic proline-rich proteins which promotes adhesion of Streptococcus gordonii to apatitic surfaces. Infect Immun. 1991 Sep;59(9):2948–2954. doi: 10.1128/iai.59.9.2948-2954.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hayashi S., Wu H. C. Lipoproteins in bacteria. J Bioenerg Biomembr. 1990 Jun;22(3):451–471. doi: 10.1007/BF00763177. [DOI] [PubMed] [Google Scholar]
  10. Jenkinson H. F. Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell surface lipoproteins. Infect Immun. 1992 Mar;60(3):1225–1228. doi: 10.1128/iai.60.3.1225-1228.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jenkinson H. F., Easingwood R. A. Insertional inactivation of the gene encoding a 76-kilodalton cell surface polypeptide in Streptococcus gordonii Challis has a pleiotropic effect on cell surface composition and properties. Infect Immun. 1990 Nov;58(11):3689–3697. doi: 10.1128/iai.58.11.3689-3697.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kolenbrander P. E., Andersen R. N. Characterization of Streptococcus gordonii (S. sanguis) PK488 adhesin-mediated coaggregation with Actinomyces naeslundii PK606. Infect Immun. 1990 Sep;58(9):3064–3072. doi: 10.1128/iai.58.9.3064-3072.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kolenbrander P. E. Surface recognition among oral bacteria: multigeneric coaggregations and their mediators. Crit Rev Microbiol. 1989;17(2):137–159. doi: 10.3109/10408418909105746. [DOI] [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Lai J. S., Sarvas M., Brammar W. J., Neugebauer K., Wu H. C. Bacillus licheniformis penicillinase synthesized in Escherichia coli contains covalently linked fatty acid and glyceride. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3506–3510. doi: 10.1073/pnas.78.6.3506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nielsen J. B., Lampen J. O. Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria. J Bacteriol. 1982 Oct;152(1):315–322. doi: 10.1128/jb.152.1.315-322.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Nyvad B., Kilian M. Comparison of the initial streptococcal microflora on dental enamel in caries-active and in caries-inactive individuals. Caries Res. 1990;24(4):267–272. doi: 10.1159/000261281. [DOI] [PubMed] [Google Scholar]
  18. Rosan B., Baker C. T., Nelson G. M., Berman R., Lamont R. J., Demuth D. R. Cloning and expression of an adhesin antigen of Streptococcus sanguis G9B in Escherichia coli. J Gen Microbiol. 1989 Mar;135(3):531–538. doi: 10.1099/00221287-135-3-531. [DOI] [PubMed] [Google Scholar]
  19. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Scannapieco F. A., Bergey E. J., Reddy M. S., Levine M. J. Characterization of salivary alpha-amylase binding to Streptococcus sanguis. Infect Immun. 1989 Sep;57(9):2853–2863. doi: 10.1128/iai.57.9.2853-2863.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wu H. C., Tokunaga M. Biogenesis of lipoproteins in bacteria. Curr Top Microbiol Immunol. 1986;125:127–157. doi: 10.1007/978-3-642-71251-7_9. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES