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. 1973 Sep;8(3):335–340. doi: 10.1128/iai.8.3.335-340.1973

Inhibition of Enzymes by Human Salivary Immunoglobulin A

Yoshio Fukui 1, Kazuhiro Fukui 1, Takafumi Moriyama 1
PMCID: PMC422853  PMID: 4354148

Abstract

Human whole saliva inhibited bacterial neuraminidases and the inhibition was found to reside in the salivary IgA fraction. Further, salivary immunoglobulin (Ig)A inhibited various bacterial enzymes and toxins: neuraminidases from Streptococcus mitis, Streptococcus sanguis, and Clostridium perfringens, hyaluronidase and chondroitin sulfatase from oral bacteria, diphtheria toxin, and streptolysin O. The inhibitory activity of salivary IgA did not correlate with that of serum on the basis of minimum inhibitory dose. A small amount of salivary IgA was required to inhibit oral bacterial neuraminidases, whereas a large amount was required to inhibit other bacterial neuraminidase. Therefore, it is concluded that the absence of neuraminidase activity of oral bacteria in whole saliva may be due to specific inhibition by salivary IgA.

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Selected References

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  1. EVANS R. T., MERGENHAGEN S. E. OCCURRENCE OF NATURAL ANTIBACTERIAL ANTIBODY IN HUMAN PAROTID FLUID. Proc Soc Exp Biol Med. 1965 Jul;119:815–819. doi: 10.3181/00379727-119-30309. [DOI] [PubMed] [Google Scholar]
  2. Fukui K., Fukui Y., Moriyama T. Neuraminidase activity in some bacteria from the human mouth. Arch Oral Biol. 1971 Nov;16(11):1361–1365. doi: 10.1016/0003-9969(71)90038-0. [DOI] [PubMed] [Google Scholar]
  3. Fukui Y., Fukui K., Moriyama T. Source of neuraminidase in human whole saliva. Infect Immun. 1973 Sep;8(3):329–334. doi: 10.1128/iai.8.3.329-334.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hershon L. E. Elaboration of hyaluronidase and chondroitin sulfatase by microorganisms inhabiting the gingival sulcus: evaluation of a screening method for periodontal disease. J Periodontol. 1971 Jan;42(1):34–36. doi: 10.1902/jop.1971.42.1.34. [DOI] [PubMed] [Google Scholar]
  5. KRAUS F. W., KONNO J. THE SALIVARY SECRETION OF ANTIBODY. Ala J Med Sci. 1965 Jan;2:15–22. [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Leah S. A., Hayes M. L. Isolation in pure culture of human oral organisms capable of producing neuraminidase. Nature. 1967 Nov 11;216(5115):599–600. doi: 10.1038/216599a0. [DOI] [PubMed] [Google Scholar]
  8. Lehner T., Clarry E. D., Cardwell J. E. Immunoglobulins in saliva and serum in dental caries. Lancet. 1967 Jun 17;1(7503):1294–1296. doi: 10.1016/s0140-6736(67)91591-7. [DOI] [PubMed] [Google Scholar]
  9. Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry. 1965 Sep;2(3):235–254. doi: 10.1016/0019-2791(65)90004-2. [DOI] [PubMed] [Google Scholar]
  10. Nijar M. S., Pritchard E. T., Dawes C., Philips S. R. Neuraminidase activity in the salivary glands of rats and human saliva. Arch Oral Biol. 1970 Jan;15(1):89–92. doi: 10.1016/0003-9969(70)90148-2. [DOI] [PubMed] [Google Scholar]
  11. Perlitsh M. J., Glickman I. Salivary neuraminidase. 3. Its relation to oral disease. J Periodontol. 1967 May-Jun;38(3):189–192. doi: 10.1902/jop.1967.38.3.189. [DOI] [PubMed] [Google Scholar]
  12. Perlitsh M. J., Glickman I. Salivary neuraminidase. I. The presence of neuraminidase in human saliva. J Periodontol. 1966 Sep-Oct;37(5):368–373. doi: 10.1902/jop.1966.37.5.368. [DOI] [PubMed] [Google Scholar]
  13. Perlitsh M. J., Glickman I. Salivary neuraminidase. II. Its source in human whole saliva. J Dent Res. 1966 Jul-Aug;45(4):1239–1239. doi: 10.1177/00220345660450044901. [DOI] [PubMed] [Google Scholar]
  14. Pinter J. K., Hayashi J. A., Bahn A. N. Carbohydrate hydrolases of oral streptococci. Arch Oral Biol. 1969 Jul;14(7):735–744. doi: 10.1016/0003-9969(69)90165-4. [DOI] [PubMed] [Google Scholar]
  15. Pinter J. K., Hayashi J. A., Bahn A. N. Extracellular streptococcal neuraminidase. J Bacteriol. 1968 Apr;95(4):1491–1492. doi: 10.1128/jb.95.4.1491-1492.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. REISSIG J. L., STORMINGER J. L., LELOIR L. F. A modified colorimetric method for the estimation of N-acetylamino sugars. J Biol Chem. 1955 Dec;217(2):959–966. [PubMed] [Google Scholar]
  17. SIMONS K., WEBER T., STIEL M., GRAESBECK R. IMMUNOELECTROPHORESIS OF HUMAN SALIVA. Acta Med Scand. 1964;175:SUPPL 412–412:257+. doi: 10.1111/j.0954-6820.1964.tb04658.x. [DOI] [PubMed] [Google Scholar]
  18. Smith R. F., Willett N. P. Rapid plate method for screening hyaluronidase and chondroitin sulfatase-producing microorganisms. Appl Microbiol. 1968 Sep;16(9):1434–1436. doi: 10.1128/am.16.9.1434-1436.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. THONARD J. C., HEFFLIN C. M., STEINBERG A. I. NEURAMINIDASE ACTIVITY IN MIXED CULTURE SUPERNATANT FLUIDS OF HUMAN ORAL BACTERIA. J Bacteriol. 1965 Mar;89:924–925. doi: 10.1128/jb.89.3.924-925.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. TOMASI T. B., Jr, TAN E. M., SOLOMON A., PRENDERGAST R. A. CHARACTERISTICS OF AN IMMUNE SYSTEM COMMON TO CERTAIN EXTERNAL SECRETIONS. J Exp Med. 1965 Jan 1;121:101–124. doi: 10.1084/jem.121.1.101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tomasi T. B., Jr, Bienenstock J. Secretory immunoglobulins. Adv Immunol. 1968;9:1–96. doi: 10.1016/s0065-2776(08)60441-1. [DOI] [PubMed] [Google Scholar]
  22. Tourville D., Bienenstock J., Tomasi T. B., Jr Natural antibodies of human serum, saliva, and urine reactive with Escherichia coli. Proc Soc Exp Biol Med. 1968 Jul;128(3):722–727. doi: 10.3181/00379727-128-33109. [DOI] [PubMed] [Google Scholar]

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