ArticleParasitology research2008
alpha14-Giardin (annexin E1) is associated with tubulin in trophozoites of Giardia lamblia and forms local slubs in the flagella.
Article in Parasitology research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2026Review
- The cytoskeleton of pathogenic protists.Bioscience reports · 2026Review
- The NLRP3 inflammasome recognizes alpha-2 and alpha-7.3 giardins and decreases the pathogenicity of Giardia duodenalis in mice.Parasites & vectors · 2023Article
- Microtubule organelles in Giardia.Advances in parasitology · 2020Review
- Article
- Immunolocalization of α18- and α12-giardin in Giardia lamblia trophozoites.Parasitology research · 2016Article
- Divergent Transcriptional Responses to Physiological and Xenobiotic Stress in Giardia duodenalis.Antimicrobial agents and chemotherapy · 2016Article
- Annexins family: insights into their functions and potential role in pathogenesis of sarcoidosis.Journal of translational medicine · 2016Review
- Giardia flagellar motility is not directly required to maintain attachment to surfaces.PLoS pathogens · 2011Article
- Life with eight flagella: flagellar assembly and division in Giardia.Current opinion in microbiology · 2010Review
- Dual acylation accounts for the localization of {alpha}19-giardin in the ventral flagellum pair of Giardia lamblia.Eukaryotic cell · 2009Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a previous study, we reported that the novel annexin XX1 (annexin E1), identical to alpha14-giardin, is specifically localized to the flagella and to the median body of the trophozoites. However, the mode of interaction and the direct partners involved remained unclear. In the present study, we show that alpha4-giardin obviously does not evenly distribute over the full length of the axonemes, but rather, resides at local slubs near the proximal part and the ends of the flagella. In immunocytochemical co-localization studies, the anti-giardin primary antibody exclusively reacted with distinct regions of the flagella in permeabilized cells, whereas the anti-tubulin antibody bound to all areas of the axonemes in the cells and to isolated cytoskeletons. Isolated cytoskeletons did not react with anti-giardin antibodies. alpha14-Giardin itself is able to assemble to multimeric structures. Taken together, our findings suggest that alpha14-giardin adheres to microtubules of the flagella via self-assembly that may regulated by Ser/Thr-phosphorylation.
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