ArticleBMC genomics2006
The SNARE protein family of Leishmania major.
Article in BMC genomics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 42 citations in OpenAlex.
- Evolutionary duplication of the leishmanial adaptor protein α-SNAP plays a role in its pathogenicity.The Journal of biological chemistry · 2025Article
- Identifying the function of genes involved in excreted vesicle formation in Acanthamoeba castellanii containing Legionella pneumophila.Parasites & vectors · 2023Article
- Hemoglobin Endocytosis and Intracellular Trafficking: A Novel Way of Heme Acquisition byPathogens (Basel, Switzerland) · 2022Review
- Cell death pathways in pathogenic trypanosomatids: lessons of (over)kill.Cell death & disease · 2019Review
- Structurally optimized analogs of the retrograde trafficking inhibitor Retro-2cycl limit Leishmania infections.PLoS neglected tropical diseases · 2017Article
- Evolution of the endomembrane systems of trypanosomatids - conservation and specialisation.Journal of cell science · 2017Article
- Exploitation of the Host Cell Membrane Fusion Machinery by Leishmania Is Part of the Infection Process.PLoS pathogens · 2016Review
- A comparative analysis of trypanosomatid SNARE proteins.Parasitology international · 2014Article
- Glycosome turnover in Leishmania major is mediated by autophagy.Autophagy · 2014Article
- Article
- Characterization of SNAREs determines the absence of a typical Golgi apparatus in the ancient eukaryote Giardia lamblia.The Journal of biological chemistry · 2008Article
- The trypanosome transcriptome is remodelled during differentiation but displays limited responsiveness within life stages.BMC genomics · 2008Article
- An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system.Molecular biology of the cell · 2007Article
- Protein turnover and differentiation in Leishmania.International journal for parasitology · 2007Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundLeishmania major is a protozoan parasite with a highly polarised cell shape that depends upon endocytosis and exocytosis from a single area of the plasma membrane, the flagellar pocket. SNAREs (soluble N-ethylmaleimide-sensitive factor adaptor proteins receptors) are key components of the intracellular vesicle-mediated transports that take place in all eukaryotic cells. They are membrane-bound proteins that facilitate the docking and fusion of vesicles with organelles. The recent availability of the genome sequence of L. major has allowed us to assess the complement of SNAREs in the parasite and to investigate their location in comparison with metazoans.
resultsBioinformatic searches of the L. major genome revealed a total of 27 SNARE domain-containing proteins that could be classified in structural groups by phylogenetic analysis. 25 of these possessed the expected features of functional SNAREs, whereas the other two could represent kinetoplastid-specific proteins that might act as regulators of the SNARE complexes. Other differences of Leishmania SNAREs were the absence of double SNARE domain-containing and of the brevin classes of these proteins. Members of the Qa group of Leishmania SNAREs showed differential expressions profiles in the two main parasite forms whereas their GFP-tagging and in vivo expression revealed localisations in the Golgi, late endosome/lysosome and near the flagellar pocket.
conclusionThe early-branching eukaryote L. major apparently possess a SNARE repertoire that equals in number the one of metazoans such as Drosophila, showing that the machinery for vesicle fusion is well conserved throughout the eukaryotes. However, the analysis revealed the absence of certain types of SNAREs found in metazoans and yeast, while suggesting the presence of original SNAREs as well as others with unusual localisation. This study also presented the intracellular localisation of the L. major SNAREs from the Qa group and reveals that these proteins could be useful as organelle markers in this parasitic protozoon.
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