Home LiteratureArticle Details
PMID: 2788139 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Characterization of salivary alpha-amylase binding to Streptococcus sanguis.

Infection and immunity ·Vol. 57 ·No. 9 ·1989-09-00 ·Pages 2853-63

Scannapieco FA, Bergey EJ, Reddy MS, Levine MJ

Abstract

The purpose of this study was to identify the major salivary components which interact with oral bacteria and to determine the mechanism(s) responsible for their binding to the bacterial surface. Strains of Streptococcus sanguis, Streptococcus mitis, Streptococcus mutans, and Actinomyces viscosus were incubated for 2 h in freshly collected human submandibular-sublingual saliva (HSMSL) or parotid saliva (HPS), and bound salivary components were eluted with 2% sodium dodecyl sulfate. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western transfer, alpha-amylase (EC 3.2.1.1) was the prominent salivary component eluted from S. sanguis. Studies with 125I-labeled HSMSL or 125I-labeled HPS also demonstrated a component with an electrophoretic mobility identical to that of alpha-amylase which bound to S. sanguis. Purified alpha-amylase from human parotid saliva was radiolabeled and found to bind to strains of S. sanguis genotypes 1 and 3 and S. mitis genotype 2, but not to strains of other species of oral bacteria. Binding of [125I]alpha-amylase to streptococci was saturable, calcium independent, and inhibitable by excess unlabeled alpha-amylases from a variety of sources, but not by secretory immunoglobulin A and the proline-rich glycoprotein from HPS. Reduced and alkylated alpha-amylase lost enzymatic and bacterial binding activities. Binding was inhibited by incubation with maltotriose, maltooligosaccharides, limit dextrins, and starch.

MeSH Terms
Adult Bacterial Adhesion Humans Iodine Radioisotopes Kinetics Male Parotid Gland Saliva/enzymology,metabolism,microbiology Salivary Proteins and Peptides/physiology Streptococcus sanguis/enzymology,metabolism,physiology Sublingual Gland Submandibular Gland alpha-Amylases/metabolism,physiology
Chemicals
Iodine Radioisotopes Salivary Proteins and Peptides alpha-Amylases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Scannapieco F A
Department of Oral Biology and Dental Research Institute, State University of New York, Buffalo 14214.
Bergey E J
Reddy M S
Levine M J
References (59)
59 references, click to expand
  1. Zooglea-forming streptococci, resembling Streptococcus sanguis, isolated from dental plaque in man.
    Odontol Revy. 1965;16(4):348-58 PMID: 5216256
  2. Quantitative gel-electrophoretic determination of serum amylase isoenzyme distributions.
    Clin Chem. 1979 Nov;25(11):1919-23 PMID: 498502
  3. The isoenzymes of human parotid amylase.
    Arch Biochem Biophys. 1970 Apr;137(2):325-39 PMID: 4985719
  4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  5. Sorption of bacteria to human enamel powder.
    Arch Oral Biol. 1970 Sep;15(9):899-903 PMID: 5273411
  6. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
    Biochemistry. 1971 Jun 22;10(13):2606-17 PMID: 4326772
  7. Inhibition of bacterial adherence by secretory immunoglobulin A: a mechanism of antigen disposal.
    Science. 1972 Aug 25;177(4050):697-9 PMID: 5054144
  8. Numerical taxonomy and laboratory identification of Bacterionema matruchotii, Rothia dentocariosa, Actinomyces naeslundii, Actinomyces viscosus, and some related bacteria.
    J Gen Microbiol. 1973 May;76(1):43-63 PMID: 4579125
  9. The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent.
    Biochem J. 1973 Jul;133(3):529-39 PMID: 4733239
  10. Evidence for post-transcriptional modification of human salivary amylase (amyl) isozymes.
    Biochem Genet. 1973 Dec;10(4):341-50 PMID: 4771318
  11. The acquired pellicle: immunofluorescent demonstration of specific proteins.
    J Oral Pathol. 1973;2(1):68-76 PMID: 4133118
  12. Growth of several cariogenic strains of oral streptococci in a chemically defined medium.
    Infect Immun. 1975 Apr;11(4):649-55 PMID: 1091546
  13. Dental caries.
    Annu Rev Med. 1975;26:121-36 PMID: 1096752
  14. Purification and properties of an alpha-amylase inhibitor from wheat.
    Biochim Biophys Acta. 1976 Jan 23;422(1):159-69 PMID: 2302
  15. Structure of the microbial flora associated with periodontal health and disease in man. A light and electron microscopic study.
    J Periodontol. 1976 Jan;47(1):1-18 PMID: 1063849
  16. Microflora in the healthy gingival sulcus in man.
    Scand J Dent Res. 1977 May;85(4):247-54 PMID: 17152
  17. Preliminary x-ray investigation on a new crystalline variety of porcine pancreatic alpha-amylase.
    FEBS Lett. 1977 Jul 1;79(1):105-8 PMID: 891918
  18. Influence of salivary components and extracellular polysaccharide synthesis from sucrose on the attachment of Streptococcus mutans 6715 to hydroxyapatite surfaces.
    Infect Immun. 1977 Nov;18(2):514-23 PMID: 924680
  19. Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans.
    Infect Immun. 1978 Jan;19(1):107-15 PMID: 415001
  20. Comparative estimates of bacterial affinities and adsorption sites on hydroxyapatite surfaces.
    Infect Immun. 1978 Mar;19(3):846-53 PMID: 640732
  21. The comparative biochemistry, physiology, and genetics of animal alpha-amylases.
    Adv Comp Physiol Biochem. 1978;7:1-103 PMID: 367107
  22. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
    Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4 PMID: 388439
  23. Aggregation and adherence of Streptococcus sanguis: role of human salivary immunoglobulin A.
    Infect Immun. 1979 Dec;26(3):1104-10 PMID: 528050
  24. The isolation and partial characterization of a sulphated glycoprotein from human whole saliva which aggregates strains of Streptococcus sanguis but not Streptococcus mutans.
    Arch Oral Biol. 1979;24(10-11):791-7 PMID: 120733
  25. Longitudinal investigation of the role of Streptococcus mutans in human fissure decay.
    Infect Immun. 1979 Nov;26(2):498-507 PMID: 397929
  26. Structural studies of the sugar chains of human parotid alpha-amylase.
    J Biol Chem. 1980 Jun 25;255(12):5635-42 PMID: 6155378
  27. Interaction of parotid saliva basic glycoprotein with Streptococcus sanguis ATCC 10557.
    J Periodontol. 1980 Sep;51(9):499-504 PMID: 6932503
  28. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A.
    Anal Biochem. 1981 Apr;112(2):195-203 PMID: 6266278
  29. Oral implantation of saliva-treated Streptococcus mutans in man.
    Arch Oral Biol. 1981;26(3):197-201 PMID: 6947727
  30. Characteristic differences between saliva-dependent aggregation and adhesion of streptococci.
    Infect Immun. 1982 Jan;35(1):86-90 PMID: 6274804
  31. Properties of cysteine-containing phosphoproteins from human submandibular-sublingual saliva.
    J Dent Res. 1982 Feb;61(2):397-9 PMID: 6948857
  32. Purification of a low-molecular-weight, mucin-type glycoprotein from human submandibular-sublingual saliva.
    Carbohydr Res. 1982 Oct 1;108(1):111-22 PMID: 7139659
  33. Characterization of a salivary agglutinin reacting with a serotype c strain of Streptococcus mutans.
    Eur J Biochem. 1983 Jun 15;133(2):255-61 PMID: 6852037
  34. Effects of alpha-amylase on in vitro growth of Legionella pneumophila.
    Infect Immun. 1983 Jul;41(1):44-9 PMID: 6190756
  35. The binding of human salivary alpha-amylase by oral strains of streptococcal bacteria.
    Arch Oral Biol. 1983;28(7):567-73 PMID: 6605739
  36. Fibronectin binding to a Streptococcus pyogenes strain.
    J Bacteriol. 1984 Feb;157(2):420-7 PMID: 6319358
  37. Neuraminidase activity: a biochemical marker to distinguish Streptococcus mitis from Streptococcus sanguis.
    J Dent Res. 1984 Feb;63(2):111-3 PMID: 6582090
  38. Agglutination of Streptococcus mutans by low-molecular-weight salivary components: effect of beta 2-microglobulin.
    Infect Immun. 1984 Nov;46(2):526-30 PMID: 6389347
  39. Binding of Escherichia coli to fibronectin. A mechanism of tissue adherence.
    J Biol Chem. 1984 Dec 10;259(23):14899-905 PMID: 6238965
  40. A comparison of bacterial aggregation induced by saliva, lysozyme, and zinc.
    Infect Immun. 1985 Apr;48(1):204-10 PMID: 3980083
  41. Conserved amino acid sequence domains in alpha-amylases from plants, mammals, and bacteria.
    Biochem Biophys Res Commun. 1985 Apr 16;128(1):470-6 PMID: 3921026
  42. Isolation and characterization of a 60-kilodalton salivary glycoprotein with agglutinating activity against strains of Streptococcus mutans.
    Infect Immun. 1986 Feb;51(2):405-13 PMID: 3002983
  43. Use of the photoaffinity cross-linking agent N-hydroxysuccinimidyl-4-azidosalicylic acid to characterize salivary-glycoprotein-bacterial interactions.
    Biochem J. 1986 Feb 15;234(1):43-8 PMID: 3707547
  44. Primary structure of human salivary alpha-amylase gene.
    Gene. 1986;41(2-3):299-304 PMID: 2423416
  45. Inhibition of the interaction of Streptococcus sanguis with hexadecane droplets by 55- and 60-kilodalton hydrophobic proteins of human saliva.
    Infect Immun. 1986 Aug;53(2):278-84 PMID: 3089934
  46. Interactions of Bacteroides gingivalis with fibrinogen.
    Infect Immun. 1986 Dec;54(3):654-8 PMID: 3096886
  47. Structural aspects of salivary glycoproteins.
    J Dent Res. 1987 Feb;66(2):436-41 PMID: 3305626
  48. Immunochemical quantitation of alpha-amylase and secretory IgA in parotid saliva from people of various ages.
    Arch Oral Biol. 1987;32(4):297-301 PMID: 3117023
  49. alpha-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate alpha-amylases.
    J Bacteriol. 1987 Dec;169(12):5745-54 PMID: 3500166
  50. Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene.
    Gene. 1987;60(1):57-64 PMID: 2450054
  51. Classification and identification of the viridans streptococci.
    Clin Microbiol Rev. 1989 Jul;2(3):315-28 PMID: 2670193
  52. Characterization of in vivo salivary-derived enamel pellicle.
    Arch Oral Biol. 1989;34(4):289-95 PMID: 2480770
  53. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  54. Device for collection of human parotid saliva.
    J Lab Clin Med. 1953 Mar;41(3):493-6 PMID: 13035284
  55. THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY.
    Biochem J. 1963 Oct;89:114-23 PMID: 14097352
  56. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY.
    Ann N Y Acad Sci. 1964 Dec 28;121:321-49 PMID: 14240533
  57. Bacteriology of human experimental gingivitis: effect of plaque age.
    Infect Immun. 1978 Sep;21(3):821-9 PMID: 711336
  58. Inhibition of Neisseria gonorrhoeae by normal human saliva.
    Br J Vener Dis. 1979 Feb;55(1):20-3 PMID: 106919
  59. Ultrastructure of the approximal dental plaque and the underlying normal and carious enamel.
    Arch Oral Biol. 1966 Sep;11(9):883-912 PMID: 5226624
Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.57.9.2853-2863.1989
Published
1989-09-00
Pages
2853-63
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC313538
Subset
IM
Grants
NIDCR NIH HHS · DE00158 · United States
NIDCR NIH HHS · DE07585 · United States
NIDCR NIH HHS · DE08240 · United States
External Links
PubMed source DOI: 10.1128/iai.57.9.2853-2863.1989 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2