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Phenotypical characteristics, biochemical pathways, molecular targets and putative role of nitric oxide-mediated programmed cell death in Leishmania

Published online by Cambridge University Press:  03 October 2006

P. HOLZMULLER
Affiliation:
Equipe 1 Rôle biologique des facteurs d'excrétion-sécrétion des leishmanies: intérêt diagnostique et immunoprophylactique, UR 008 Pathogénie des Trypanosomatidae, IRD (Institut de Recherche pour le Développement), B.P. 64501, 911 avenue Agropolis, 34394 Montpellier cedex 5, France
R. BRAS-GONÇALVES
Affiliation:
Equipe 1 Rôle biologique des facteurs d'excrétion-sécrétion des leishmanies: intérêt diagnostique et immunoprophylactique, UR 008 Pathogénie des Trypanosomatidae, IRD (Institut de Recherche pour le Développement), B.P. 64501, 911 avenue Agropolis, 34394 Montpellier cedex 5, France
J.-L. LEMESRE
Affiliation:
Equipe 1 Rôle biologique des facteurs d'excrétion-sécrétion des leishmanies: intérêt diagnostique et immunoprophylactique, UR 008 Pathogénie des Trypanosomatidae, IRD (Institut de Recherche pour le Développement), B.P. 64501, 911 avenue Agropolis, 34394 Montpellier cedex 5, France
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Abstract

Nitric oxide (NO) has been demonstrated to be the principal effector molecule mediating intracellular killing of Leishmania, both in vitro and in vivo. We investigated the type of cell death process induced by NO for the intracellular amastigote stage of the protozoa Leishmania. Specific detection methods revealed a rapid and extensive cell death with morphological features of apoptosis in axenic amastigotes exposed to NO donors, in intracellular amastigotes inside in vitro – activated mouse macrophages and also in activated macrophages of regressive lesions in a leishmaniasis-resistant mouse model. We extended our investigations to the dog, a natural host-reservoir of Leishmania parasites, by demonstrating that co-incubation of infected macrophages with autologous lymphocytes derived from dogs immunised with purified excreted-secreted antigens of Leishmania resulted in a significant NO-mediated apoptotic cell death of intracellular amastigotes. From the biochemical point of view, NO-mediated Leishmania amastigotes apoptosis did not seem to be controlled by caspase activity as indicated by the lack of effect of cell permeable inhibitors of caspases and cysteine proteases, in contrast to specific proteasome inhibitors, such as lactacystin or calpain inhibitor I. Moreover, addition of the products of two NO molecular targets, cis-aconitase and glyceraldehyde-3-phosphate dehydrogenase, also had an inhibitory effect on the cell death induced by NO. Interestingly, activities of these two enzymes plus 6-phosphogluconate dehydrogenase, parasitic enzymes involved in both glycolysis and respiration processes, are overexpressed in amastigotes selected for their NO resistance. This review focuses on cell death of the intracellular stage of the pathogen Leishmania induced by nitrogen oxides and gives particular attention to the biochemical pathways and the molecular targets potentially involved. Questions about the role of Leishmania amastigotes NO-mediated apoptosis in the overall infection process are raised and discussed.

Information

Type
Research Article
Copyright
© 2006 Cambridge University Press
Figure 0

Fig. 1. Immunological determinants influencing Leishmania infection. Cytokines expressed by macrophages, dendritic cells and T- and B-lymphocytes determine the outcome of Leishmania parasites: from survival and proliferation to death. What role plays parasite apoptosis in this balance? Th: T helper, Thp: precursor T helper, Treg: T regulator, NK: natural killer, CD: cluster of differentiation, IL: interleukine, IFN-α: interferon α, IFN-γ: interferon γ, TNF-α: tumour necrosis factor α, TGF-β: transforming growth factor β, MHC: major histocompatibility complex, NOS: nitric oxide synthase, NO: nitric oxide.

Figure 1

Fig. 2. NO-mediated programmed cell death exhibiting morphological features of apoptosis in Leishmania amastigotes. Control versus NO donor-treated axenic amastigotes DNA banding pattern in ethidium bromide-stained agarose gel (A), recognition of apoptotic DNA strand breaks by the in situ Terminal deoxynucleotidyl Transferase-mediated dUTP Nick-End Labeling (TUNEL assay kit, Alexis Biochemicals) in control versus NO donor-treated axenic amastigotes (B) and in intracellular amastigotes within control versus NO producing mouse macrophages (D), apoptotic fluorescent YOPRO-1 probe staining in flow cytofluorometry analysis of control versus NO donor-treated (6 hours with 5 mM acidified sodium nitrite) axenic amastigotes (C) and in situ in intracellullar amastigotes within control versus NO producing dog macrophages (E). Evolution of footpad lesion size and nitrate/nitrite levels in sera of Balb/C and C57/Black6 mice infected with Leishmania amazonensis (F) and in situ TUNEL in histological thin cryosections counterstained with Giemsa of footpad lesions of Balb/C (G) and C57/Black6 (H) mice.

Figure 2

Fig. 3. NO molecular targets in Leishmania. Proteinase activities in gelatin-copolymerised SDS-PAGE stained by Coomassie blue of L. amazonensis amastigotes protein lysates either incubated in the presence or absence of 5 mM acidified sodium nitrite during gel revelation steps (A) or prepared from axenic parasites cultured for 4 hours in acidified PBS in the absence or presence of 5 mM sodium nitrite (B). Cis-aconitase activity of N2- versus NO-treated promastigotes (P) and axenic amastigotes (A) of L. amazonensis (L. amaz.) and L. mexicana (L. mex.) by multilocus enzyme electrophoresis (MLEE) (C). Apoptosis of L. amazonensis axenic amastigotes cultured in the presence of NO donor in a medium supplemented by either cis-aconitate (product of cis-aconitase) or 1,3-bisphosphoglycerate (product of glyceraldehyde-3-phosphate dehydrogenase) (D). MLEE profiles revealed with the cis-aconitase hydratase (E.C.4.2.1.3), glyceraldehyde-3-phosphate dehydrogenase (E.C.1.2.1.12), 6-phosphogluconate dehydrogenase (EC1.1.1.44) of wild-type amastigotes (LiWT) and amastigotes resistant to 50 mM (LiNOR50) and to 100 mM (LiNOR100) DETA/NONOate (E).