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. 1991 Feb;59(2):696–699. doi: 10.1128/iai.59.2.696-699.1991

Effect of sulfide ions on complement factor C3.

M Granlund-Edstedt 1, E Johansson 1, R Claesson 1, J Carlsson 1
PMCID: PMC257813  PMID: 1987085

Abstract

In infected sites such as the gingival pockets of patients with periodontal disease, sulfide levels up to 1 mmol/liter may be reached. There is little information, however, on how sulfide may interact with the host defense. In a previous study (R. Claesson, M. Granlund-Edstedt, S. Persson, and J. Carlsson, Infect. Immun. 57:2776-2781, 1989), it was shown that polymorphonuclear leukocytes were able to kill bacteria in the presence of 1 mM sulfide. However, sulfide seemed to interfere with the opsonization of the bacteria. It has been claimed that sulfide may be toxic by splitting disulfide bonds of proteins. In the present study, serum was exposed to 2 mM sulfide under anaerobic conditions, and the capacity of sulfide to split disulfide bonds of 10 serum proteins involved in opsonization was evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodetection of the proteins after blotting. Sulfide had a low capacity to split the disulfide bonds of most proteins. Sulfide had, however, a pronounced effect on the complement component C3 in the form of C3bi. Sulfide released the C-terminal region of the alpha chain from C3bi. When C3 opsonizes bacteria, it is this region of C3bi which binds to complement receptor 3 (CR3) of the polymorphonuclear leukocytes. If sulfide has the same effect on C3bi deposited on the bacterial surface as it has on C3bi in solution, it will annihilate the very important contribution of C3bi to opsonization.

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Selected References

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

  1. Beauchamp R. O., Jr, Bus J. S., Popp J. A., Boreiko C. J., Andjelkovich D. A. A critical review of the literature on hydrogen sulfide toxicity. Crit Rev Toxicol. 1984;13(1):25–97. doi: 10.3109/10408448409029321. [DOI] [PubMed] [Google Scholar]
  2. Cavallini D., Federici G., Barboni E. Interaction of proteins with sulfide. Eur J Biochem. 1970 May 1;14(1):169–174. doi: 10.1111/j.1432-1033.1970.tb00275.x. [DOI] [PubMed] [Google Scholar]
  3. Claesson R., Granlund-Edstedt M., Persson S., Carlsson J. Activity of polymorphonuclear leukocytes in the presence of sulfide. Infect Immun. 1989 Sep;57(9):2776–2781. doi: 10.1128/iai.57.9.2776-2781.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fong J. S., Renaud L. A hemolytic plate method for alternative-pathway complement activity assay. Am J Clin Pathol. 1978 Feb;69(2):156–160. doi: 10.1093/ajcp/69.2.156. [DOI] [PubMed] [Google Scholar]
  5. Janatova J. Detection of disulphide bonds and localization of interchain linkages in the third (C3) and the fourth (C4) components of human complement. Biochem J. 1986 Feb 1;233(3):819–825. doi: 10.1042/bj2330819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kadota H., Ishida Y. Production of volatile sulfur compounds by microorganisms. Annu Rev Microbiol. 1972;26:127–138. doi: 10.1146/annurev.mi.26.100172.001015. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Morhart R. E., Mata L. J., Sinskey A. J., Harris R. S. A microbiological and biochemical study of gingival crevice debris obtained from Guatemalan Mayan Indians. J Periodontol. 1970 Nov;41(11):644–649. doi: 10.1902/jop.1970.41.11.644. [DOI] [PubMed] [Google Scholar]
  9. Müller-Eberhard H. J. Molecular organization and function of the complement system. Annu Rev Biochem. 1988;57:321–347. doi: 10.1146/annurev.bi.57.070188.001541. [DOI] [PubMed] [Google Scholar]
  10. Persson S., Claesson R., Carlsson J. The capacity of subgingival microbiotas to produce volatile sulfur compounds in human serum. Oral Microbiol Immunol. 1989 Sep;4(3):169–172. doi: 10.1111/j.1399-302x.1989.tb00246.x. [DOI] [PubMed] [Google Scholar]
  11. SIEGEL L. M. A DIRECT MICRODETERMINATION FOR SULFIDE. Anal Biochem. 1965 Apr;11:126–132. doi: 10.1016/0003-2697(65)90051-5. [DOI] [PubMed] [Google Scholar]
  12. Towbin H., Staehelin T., Gordon J. 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):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Truedsson L., Sjöholm A. G., Laurell A. B. Screening for deficiencies in the classical and alternative pathways of complement by hemolysis in gel. Acta Pathol Microbiol Scand C. 1981 Jun;89(3):161–166. doi: 10.1111/j.1699-0463.1981.tb02680.x. [DOI] [PubMed] [Google Scholar]
  14. Valentine W. N., Toohey J. I., Paglia D. E., Nakatani M., Brockway R. A. Modification of erythrocyte enzyme activities by persulfides and methanethiol: possible regulatory role. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1394–1398. doi: 10.1073/pnas.84.5.1394. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Warenycia M. W., Goodwin L. R., Benishin C. G., Reiffenstein R. J., Francom D. M., Taylor J. D., Dieken F. P. Acute hydrogen sulfide poisoning. Demonstration of selective uptake of sulfide by the brainstem by measurement of brain sulfide levels. Biochem Pharmacol. 1989 Mar 15;38(6):973–981. doi: 10.1016/0006-2952(89)90288-8. [DOI] [PubMed] [Google Scholar]
  16. Warenycia M. W., Smith K. A., Blashko C. S., Kombian S. B., Reiffenstein R. J. Monoamine oxidase inhibition as a sequel of hydrogen sulfide intoxication: increases in brain catecholamine and 5-hydroxytryptamine levels. Arch Toxicol. 1989;63(2):131–136. doi: 10.1007/BF00316435. [DOI] [PubMed] [Google Scholar]
  17. Wright S. D., Reddy P. A., Jong M. T., Erickson B. W. C3bi receptor (complement receptor type 3) recognizes a region of complement protein C3 containing the sequence Arg-Gly-Asp. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1965–1968. doi: 10.1073/pnas.84.7.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Wright S. D., Weitz J. I., Huang A. J., Levin S. M., Silverstein S. C., Loike J. D. Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7734–7738. doi: 10.1073/pnas.85.20.7734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. de Bruijn M. H., Fey G. H. Human complement component C3: cDNA coding sequence and derived primary structure. Proc Natl Acad Sci U S A. 1985 Feb;82(3):708–712. doi: 10.1073/pnas.82.3.708. [DOI] [PMC free article] [PubMed] [Google Scholar]

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