Effect of Legionella pneumophila cytotoxic protease on human neutrophil and monocyte function

C Rechnitzer; A Kharazmi

Effect of Legionella pneumophila cytotoxic protease on human neutrophil and monocyte function

C Rechnitzer, A Kharazmi

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

24 Citationer (Scopus)

Abstract

Udgivelsesdato: 1992-Feb

Originalsprog	Engelsk
Tidsskrift	Microbial Pathogenesis
Vol/bind	12
Udgave nummer	2
Sider (fra-til)	115-25
Antal sider	10
ISSN	0882-4010
Status	Udgivet - 1992

Bibliografisk note

Keywords: Bacterial Proteins; Chemotaxis; Humans; Kinetics; Legionella pneumophila; Listeria monocytogenes; Metalloendopeptidases; Monocytes; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Phagocytosis; Respiratory Burst

Citationsformater

@article{491ac8601fc311df8ed1000ea68e967b,

title = "Effect of Legionella pneumophila cytotoxic protease on human neutrophil and monocyte function",

abstract = "The extracellular metalloprotease of Legionella pneumophila, also called tissue-destructive protease or major secretory protein, has been proposed as one of the virulence factors of this organism. Considering the decisive role played by the phagocytic cells in host defense against Legionella infection, we investigated the effect of this protease on the function of human neutrophils and monocytes. L. pneumophila protease inhibited the chemotactic response of neutrophils to F-Met-Leu-Phe and zymosan-activated serum in a concentration-dependent and heat-labile manner. A direct effect of the protease on the chemotactic activity of neutrophils was demonstrated by the continued inhibition of neutrophil chemotaxis when the protease was removed following pre-incubation of the cells. In contrast, the enzyme had no effect on monocyte chemotaxis. The protease inhibited, also in a concentration-dependent and heat-labile manner, the binding of F-Met-Leu-Phe to both cell types. Neutrophil and monocyte oxidative burst response, as measured by superoxide release and chemiluminescence response, was not significantly affected by the enzyme. A slight enhancement of PMA-stimulated superoxide release was induced by the protease in both cell types. Lastly, the protease inhibited the killing of Listeria monocytogenes by neutrophils or monocytes. Inhibition of Listeria killing was concentration-dependent, heat-labile, and did not require the presence of the enzyme in the bactericidal assay. The inhibitory activity of L. pneumophila protease on neutrophil chemotaxis and on the listericidal activity of human neutrophils and monocytes demonstrated in this study provides evidence for a role of this enzyme in the pathogenesis of Legionnaires' disease.",

author = "C Rechnitzer and A Kharazmi",

note = "Keywords: Bacterial Proteins; Chemotaxis; Humans; Kinetics; Legionella pneumophila; Listeria monocytogenes; Metalloendopeptidases; Monocytes; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Phagocytosis; Respiratory Burst",

year = "1992",

language = "English",

volume = "12",

pages = "115--25",

journal = "Microbial Pathogenesis",

issn = "0882-4010",

publisher = "Academic Press",

number = "2",

}

TY - JOUR

T1 - Effect of Legionella pneumophila cytotoxic protease on human neutrophil and monocyte function

AU - Rechnitzer, C

AU - Kharazmi, A

N1 - Keywords: Bacterial Proteins; Chemotaxis; Humans; Kinetics; Legionella pneumophila; Listeria monocytogenes; Metalloendopeptidases; Monocytes; N-Formylmethionine Leucyl-Phenylalanine; Neutrophils; Phagocytosis; Respiratory Burst

PY - 1992

Y1 - 1992

N2 - The extracellular metalloprotease of Legionella pneumophila, also called tissue-destructive protease or major secretory protein, has been proposed as one of the virulence factors of this organism. Considering the decisive role played by the phagocytic cells in host defense against Legionella infection, we investigated the effect of this protease on the function of human neutrophils and monocytes. L. pneumophila protease inhibited the chemotactic response of neutrophils to F-Met-Leu-Phe and zymosan-activated serum in a concentration-dependent and heat-labile manner. A direct effect of the protease on the chemotactic activity of neutrophils was demonstrated by the continued inhibition of neutrophil chemotaxis when the protease was removed following pre-incubation of the cells. In contrast, the enzyme had no effect on monocyte chemotaxis. The protease inhibited, also in a concentration-dependent and heat-labile manner, the binding of F-Met-Leu-Phe to both cell types. Neutrophil and monocyte oxidative burst response, as measured by superoxide release and chemiluminescence response, was not significantly affected by the enzyme. A slight enhancement of PMA-stimulated superoxide release was induced by the protease in both cell types. Lastly, the protease inhibited the killing of Listeria monocytogenes by neutrophils or monocytes. Inhibition of Listeria killing was concentration-dependent, heat-labile, and did not require the presence of the enzyme in the bactericidal assay. The inhibitory activity of L. pneumophila protease on neutrophil chemotaxis and on the listericidal activity of human neutrophils and monocytes demonstrated in this study provides evidence for a role of this enzyme in the pathogenesis of Legionnaires' disease.

AB - The extracellular metalloprotease of Legionella pneumophila, also called tissue-destructive protease or major secretory protein, has been proposed as one of the virulence factors of this organism. Considering the decisive role played by the phagocytic cells in host defense against Legionella infection, we investigated the effect of this protease on the function of human neutrophils and monocytes. L. pneumophila protease inhibited the chemotactic response of neutrophils to F-Met-Leu-Phe and zymosan-activated serum in a concentration-dependent and heat-labile manner. A direct effect of the protease on the chemotactic activity of neutrophils was demonstrated by the continued inhibition of neutrophil chemotaxis when the protease was removed following pre-incubation of the cells. In contrast, the enzyme had no effect on monocyte chemotaxis. The protease inhibited, also in a concentration-dependent and heat-labile manner, the binding of F-Met-Leu-Phe to both cell types. Neutrophil and monocyte oxidative burst response, as measured by superoxide release and chemiluminescence response, was not significantly affected by the enzyme. A slight enhancement of PMA-stimulated superoxide release was induced by the protease in both cell types. Lastly, the protease inhibited the killing of Listeria monocytogenes by neutrophils or monocytes. Inhibition of Listeria killing was concentration-dependent, heat-labile, and did not require the presence of the enzyme in the bactericidal assay. The inhibitory activity of L. pneumophila protease on neutrophil chemotaxis and on the listericidal activity of human neutrophils and monocytes demonstrated in this study provides evidence for a role of this enzyme in the pathogenesis of Legionnaires' disease.

M3 - Journal article

C2 - 1584005

SN - 0882-4010

VL - 12

SP - 115

EP - 125

JO - Microbial Pathogenesis

JF - Microbial Pathogenesis

IS - 2

ER -