The SNARE protein family of Leishmania major

Besteiro, S., Coombs, G.H. and Mottram, J.C. (2006) The SNARE protein family of Leishmania major. BMC Genomics, 7(250),

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Abstract

<b>Background</b> <i>Leishmania major</i> 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 <i>N</i>-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 <i>L. major</i> has allowed us to assess the complement of SNAREs in the parasite and to investigate their location in comparison with metazoans. <b>Results</b> Bioinformatic searches of the <i>L. major</i> 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 <i>Leishmania</i> SNAREs were the absence of double SNARE domain-containing and of the brevin classes of these proteins. Members of the Qa group of <i>Leishmania</i> SNAREs showed differential expressions profiles in the two main parasite forms whereas their GFP-tagging and <i>in vivo</i> expression revealed localisations in the Golgi, late endosome/lysosome and near the flagellar pocket. <b>Conclusion</b> The early-branching eukaryote <i>L. major</i> apparently possess a SNARE repertoire that equals in number the one of metazoans such as <i>Drosophila</i>, 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 <i>L. major</i> SNAREs from the Qa group and reveals that these proteins could be useful as organelle markers in this parasitic protozoon.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Mottram, Professor Jeremy and Coombs, Professor Graham
Authors: Besteiro, S., Coombs, G.H., and Mottram, J.C.
Subjects:Q Science > QR Microbiology > QR355 Virology
College/School:College of Medical Veterinary and Life Sciences
College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:BMC Genomics
Publisher:Biomed Central
ISSN:0009-2258
First Published:First published in BMC Genomics 7(250)

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
297261Post-genomic analysis of cysteine protease function in Leishmania parasitesJeremy MottramMedical Research Council (MRC)G0000508Infection Immunity and Inflammation Life Sciences