Giardia lamblia EB1 is a functional homolog of yeast Bim1p that binds to microtubules

Juri Kim, Seobo Sim, Junwon Kim, Kiwon Song, Tai Soon Yong, Soon Jung Park

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11 Citations (Scopus)


Giardia lamblia, with two nuclei and a distinct polarized morphology, is an interesting organism for investigating how distribution of its microtubule (MT) is controlled during its cell cycle. In this study, we identified the end-binding protein 1 (EB1) of G. lamblia, a well-known microtubule-associated protein that organizes MTs in eukaryotes. Immunofluorescence assays using recombinant EB1 (rEB1)-specific antibodies demonstrated EB1 localization in nuclear membrane as well as in some cytoskeletal structures such as axomenes and median bodies of trophozoites of G. lamblia. Complementation experiments using the BIM1 knock-out mutant of yeast, the yeast homolog of mammalian EB1, showed that giardial EB1 was able to carry out a homologous function in controlling MT dynamics. In addition, rEB1 of G. lamblia co-precipitated with MTs by an in vitro binding assay, thereby demonstrating that G. lamblia EB1 is a MT-associated protein. These results, taken together, suggest that G. lamblia EB1 is a functional homolog of eukaryotic EB1 and is likely to be a determinant for MT distribution.

Original languageEnglish
Pages (from-to)465-471
Number of pages7
JournalParasitology International
Issue number4
Publication statusPublished - 2008 Dec

Bibliographical note

Funding Information:
This work was supported by a grant from the Anti-Communicable Diseases Program of the National Institute of Health (NIH 348-6111-215), Ministry of Health and Welfare, Korea, and partially by the Seoul R&BD program (grant 10580).

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Infectious Diseases


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