Transglutaminase in Plasmodium parasites: activity and putative role in oocysts and blood stages

Transglutaminase was identified in malaria parasites by immunofluorescence microscopy using α-transglutaminase antiserum. Functional enzyme was demonstrated in vivo and in vitro using labeled polyamines that become incorporated into protein substrates through TGase activity. In Plasmodium falciparum...

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Bibliographic Details
Published in:Molecular and biochemical parasitology 2001-10, Vol.117 (2), p.161-168
Main Authors: Adini, Avner, Krugliak, Miriam, Ginsburg, Hagai, Li, Lili, Lavie, Lena, Warburg, Alon
Format: Article
Language:English
Subjects:
Aedes - parasitology
Animals
Calcium - metabolism
Calcium-independent activity
Chickens - parasitology
Culicidae
Erythrocytes - parasitology
Fluorescein-cadaverine
Humans
Malaria, Avian - parasitology
Malaria, Falciparum - parasitology
Plasmodium
Plasmodium falciparum
Plasmodium falciparum - enzymology
Plasmodium falciparum - growth & development
Plasmodium gallinaceum
Plasmodium gallinaceum - enzymology
Plasmodium gallinaceum - growth & development
Transglutaminase
Transglutaminases - antagonists & inhibitors
Transglutaminases - metabolism
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Summary:Transglutaminase was identified in malaria parasites by immunofluorescence microscopy using α-transglutaminase antiserum. Functional enzyme was demonstrated in vivo and in vitro using labeled polyamines that become incorporated into protein substrates through TGase activity. In Plasmodium falciparum intraerythrocytic parasites, transglutaminase activity was stage-dependent: it was weak in ring-forms but much stronger in trophozoites and schizonts. High levels of activity were detected in P. gallinaceum zygotes and ookinetes and in capsules of oocysts developing on mosquito midguts. Unlike most known transglutaminases, the enzymatic activity in Plasmodium was Ca 2+-independent. Furthermore, levels of activity were similar at 37 and 26 °C. Parasite transglutaminase may be responsible for the modification of erythrocytic cytoskeleton in infected cells and it may facilitate the construction of oocyst capsules by cross-linking mosquito-derived basement membrane components with Plasmodium-derived proteins.
ISSN:0166-6851
1872-9428
DOI:10.1016/S0166-6851(01)00345-0