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

Avner Adini, Miriam Krugliak, Hagai Ginsburg, Lili Li, Lena Lavie, Alon Warburg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


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 Ca2+-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.

Original languageAmerican English
Pages (from-to)161-168
Number of pages8
JournalMolecular and Biochemical Parasitology
Issue number2
StatePublished - 2001

Bibliographical note

Funding Information:
This research was supported by a grant from the Center for the Study of Emerging Diseases and US–Israel Binantional Foundation (BSF) Grant No. 93-00020/1.


  • Calcium-independent activity
  • Fluorescein-cadaverine
  • Plasmodium
  • Transglutaminase


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