Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin

M. Nandoskar, A. Ferrante, E. J. Bates, N. Hurst, J. C. Paton

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The interaction between the pneumococcal toxin pneumolysin and human monocytes was examined. At non-cytotoxic concentrations (0.5-2.5 HU/106 cells) pneumolysin depressed the oxygen-dependent respiratory burst in monocytes, induced by opsonized zymosan or phorbol myristate acetate (PMA). This included depressed hexose-monophosphate shunt activity and hydrogen peroxide production. The toxin also depressed the ability of monocytes to degranulate (measured by release of lysozyme) in response to the above stimuli. Phospholipid transmethylation was also markedly decreased by pretreating monocytes with pneumolysin. These effects on monocytes functions were accompanied by a decreased ability of pneumolysin-treated monocytes to kill Streptococcus pneumoniae, the organism that produces the toxin. Cholesterol, which inhibits the haemolytic activity of the toxin, was shown to abrogate the effects of pneumolysin on monocytes.

LanguageEnglish
Pages515-520
Number of pages6
JournalImmunology
Volume59
Issue number4
Publication statusPublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • Immunology

Cite this

Nandoskar, M., Ferrante, A., Bates, E. J., Hurst, N., & Paton, J. C. (1986). Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin. Immunology, 59(4), 515-520.
Nandoskar, M. ; Ferrante, A. ; Bates, E. J. ; Hurst, N. ; Paton, J. C. / Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin. In: Immunology. 1986 ; Vol. 59, No. 4. pp. 515-520.
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abstract = "The interaction between the pneumococcal toxin pneumolysin and human monocytes was examined. At non-cytotoxic concentrations (0.5-2.5 HU/106 cells) pneumolysin depressed the oxygen-dependent respiratory burst in monocytes, induced by opsonized zymosan or phorbol myristate acetate (PMA). This included depressed hexose-monophosphate shunt activity and hydrogen peroxide production. The toxin also depressed the ability of monocytes to degranulate (measured by release of lysozyme) in response to the above stimuli. Phospholipid transmethylation was also markedly decreased by pretreating monocytes with pneumolysin. These effects on monocytes functions were accompanied by a decreased ability of pneumolysin-treated monocytes to kill Streptococcus pneumoniae, the organism that produces the toxin. Cholesterol, which inhibits the haemolytic activity of the toxin, was shown to abrogate the effects of pneumolysin on monocytes.",
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Nandoskar, M, Ferrante, A, Bates, EJ, Hurst, N & Paton, JC 1986, 'Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin', Immunology, vol. 59, no. 4, pp. 515-520.

Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin. / Nandoskar, M.; Ferrante, A.; Bates, E. J.; Hurst, N.; Paton, J. C.

In: Immunology, Vol. 59, No. 4, 1986, p. 515-520.

Research output: Contribution to journalArticle

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T1 - Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin

AU - Nandoskar, M.

AU - Ferrante, A.

AU - Bates, E. J.

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AU - Paton, J. C.

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AB - The interaction between the pneumococcal toxin pneumolysin and human monocytes was examined. At non-cytotoxic concentrations (0.5-2.5 HU/106 cells) pneumolysin depressed the oxygen-dependent respiratory burst in monocytes, induced by opsonized zymosan or phorbol myristate acetate (PMA). This included depressed hexose-monophosphate shunt activity and hydrogen peroxide production. The toxin also depressed the ability of monocytes to degranulate (measured by release of lysozyme) in response to the above stimuli. Phospholipid transmethylation was also markedly decreased by pretreating monocytes with pneumolysin. These effects on monocytes functions were accompanied by a decreased ability of pneumolysin-treated monocytes to kill Streptococcus pneumoniae, the organism that produces the toxin. Cholesterol, which inhibits the haemolytic activity of the toxin, was shown to abrogate the effects of pneumolysin on monocytes.

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