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. 1989 May;67(1):32–37.

Proteinase-like activity in the cytotoxic factor produced by T cells during dengue virus infection.

M Khanna 1, U C Chaturvedi 1, B R Srinivasa 1, K R Swaminathan 1, A Mathur 1
PMCID: PMC1385284  PMID: 2661415

Abstract

Dengue type 2 virus (DV)-induced cytotoxic factor (CF) or the virus-primed spleen cell capable of secreting CF were treated with various proteinase inhibitors and their activity was assayed. It was observed that the cytotoxic activity of CF was inhibited significantly, in a dose-dependent manner, by pretreatment with bovine pancreatic trypsin inhibitor (BPTI) and phenylmethylsulphonyl fluoride (PMSF), to a lesser extent by soya-bean trypsin inhibitor (SBTI) and leupeptin and not at all by 1,10-phenanthroline (OP). Similar effects were observed by pretreatment of DV-primed spleen cells. Amidolytic activity of CF or its purified fractions was assayed using twelve chromogenic peptide substrates and all the substrates were hydrolysed to the varying extent. The amidolytic activity of CF was also inhibited by pretreatment with proteinase inhibitors. Thus, CF could be a proteinase with the distinction of having a broad spectrum of activity.

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Selected References

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

  1. Adams D. O. Effector mechanisms of cytolytically activated macrophages. I. Secretion of neutral proteases and effect of protease inhibitors. J Immunol. 1980 Jan;124(1):286–292. [PubMed] [Google Scholar]
  2. Chang T. W., Eisen H. N. Effects of N alpha-tosyl-L-lysyl-chloromethylketone on the activity of cytotoxic T lymphocytes. J Immunol. 1980 Mar;124(3):1028–1033. [PubMed] [Google Scholar]
  3. Chaturvedi U. C., Bhargava A., Mathur A. Production of cytotoxic factor in the spleen of dengue virus-infected mice. Immunology. 1980 Aug;40(4):665–671. [PMC free article] [PubMed] [Google Scholar]
  4. Chaturvedi U. C., Dalakoti H., Mathur A. Characterization of the cytotoxic factor produced in the spleen of dengue virus-infected mice. Immunology. 1980 Oct;41(2):387–392. [PMC free article] [PubMed] [Google Scholar]
  5. Chaturvedi U. C., Gulati L., Mathur A. Inhibition of E-rosette formation and phagocytosis by human blood leucocytes after treatment with the dengue virus-induced cytotoxic factor. Immunology. 1982 Apr;45(4):679–685. [PMC free article] [PubMed] [Google Scholar]
  6. Chaturvedi U. C., Nagar R., Gulati L., Mathur A. Variable effects of dengue virus-induced cytotoxic factors on different subpopulations of macrophages. Immunology. 1987 Jul;61(3):297–301. [PMC free article] [PubMed] [Google Scholar]
  7. Chaturvedi U. C., Nagar R., Mathur A. Effect of dengue virus infection on Fc-receptor functions of mouse macrophages. J Gen Virol. 1983 Nov;64(Pt 11):2399–2407. doi: 10.1099/0022-1317-64-11-2399. [DOI] [PubMed] [Google Scholar]
  8. Chaturvedi U. C., Tandon H. O., Mathur A. Control of in vitro and in vivo spread of coxsackievirus B4 infection by sensitized spleen cells and antibody. J Infect Dis. 1978 Aug;138(2):181–190. doi: 10.1093/infdis/138.2.181. [DOI] [PubMed] [Google Scholar]
  9. Chaturvedi U. C., Tandon P., Mathur A. Effect of immunosuppression on dengue virus infection in mice. J Gen Virol. 1977 Sep;36(3):449–458. doi: 10.1099/0022-1317-36-3-449. [DOI] [PubMed] [Google Scholar]
  10. Gulati L., Chaturvedi U. C., Mathur A. Characterization of the cytotoxin produced by macrophages in response to dengue virus-induced cytotoxic factor. Br J Exp Pathol. 1983 Apr;64(2):185–190. [PMC free article] [PubMed] [Google Scholar]
  11. Gulati L., Chaturvedi U. C., Mathur A. Depressed macrophage functions in dengue virus-infected mice: role of the cytotoxic factor. Br J Exp Pathol. 1982 Apr;63(2):194–202. [PMC free article] [PubMed] [Google Scholar]
  12. Iwata M., Munoz J. J., Ishizaka K. Modulation of the biologic activities of IgE-binding factor. IV. Identification of glycosylation-enhancing factor as a kallikrein-like enzyme. J Immunol. 1983 Oct;131(4):1954–1960. [PubMed] [Google Scholar]
  13. Kramer M. D., Binninger L., Schirrmacher V., Moll H., Prester M., Nerz G., Simon M. M. Characterization and isolation of a trypsin-like serine protease from a long-term culture cytolytic T cell line and its expression by functionally distinct T cells. J Immunol. 1986 Jun 15;136(12):4644–4651. [PubMed] [Google Scholar]
  14. Ku G. S., Quigley J. P., Sultzer B. M. The inhibition of the mitogenic stimulation of B lymphocytes by a serine protease inhibitor: commitment to proliferation correlates with an enhanced expression of a cell-associated arginine-specific serine enzyme. J Immunol. 1983 Nov;131(5):2494–2499. [PubMed] [Google Scholar]
  15. Nagar R., Chaturvedi U. C., Mathur A. Effect of dengue virus-induced cytotoxic factor on Fc-receptor functions of mouse macrophages. Br J Exp Pathol. 1984 Feb;65(1):11–17. [PMC free article] [PubMed] [Google Scholar]
  16. Pasternack M. S., Eisen H. N. A novel serine esterase expressed by cytotoxic T lymphocytes. 1985 Apr 25-May 1Nature. 314(6013):743–745. doi: 10.1038/314743a0. [DOI] [PubMed] [Google Scholar]
  17. Redelman D., Hudig D. The mechanism of cell-mediated cytotoxicity. I. Killing by murine cytotoxic T lymphocytes requires cell surface thiols and activated proteases. J Immunol. 1980 Feb;124(2):870–878. [PubMed] [Google Scholar]
  18. Shukla M. I., Dalakoti H., Chaturvedi U. C. Ly phenotype of T lymphocytes producing dengue virus-induced immunosuppressive factors. Indian J Exp Biol. 1982 Jul;20(7):525–528. [PubMed] [Google Scholar]
  19. Simon M. M., Fruth U., Simon H. G., Kramer M. D. A specific serine proteinase is inducible in Lyt-2+,L3T4- and Lyt-2-,L3T4+ T cells in vitro but is mainly associated with Lyt-2+,L3T4- effector cells in vivo. Eur J Immunol. 1986 Dec;16(12):1559–1568. doi: 10.1002/eji.1830161215. [DOI] [PubMed] [Google Scholar]
  20. Simon M. M., Simon H. G., Fruth U., Epplen J., Müller-Hermelink H. K., Kramer M. D. Cloned cytolytic T-effector cells and their malignant variants produce an extracellular matrix degrading trypsin-like serine proteinase. Immunology. 1987 Feb;60(2):219–230. [PMC free article] [PubMed] [Google Scholar]
  21. Vischer T. L. Stimulation of mouse B lymphocytes by trypsin. J Immunol. 1974 Jul;113(1):58–62. [PubMed] [Google Scholar]
  22. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  23. Young J. D., Liu C. C. Multiple mechanisms of lymphocyte-mediated killing. Immunol Today. 1988 May;9(5):140–144. doi: 10.1016/0167-5699(88)91201-7. [DOI] [PubMed] [Google Scholar]

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