Syracuse

Identification of a new developmentally regulated Leishmania major large RAB GTPase.

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Chenik, Mehdi | Chaabouni, Noura | Ben Achour-Chenik, Yosser | Ouakad, Meriem | Lakhal-Naouar, Inès | Louzir, Hechmi | Dellagi, Koussay

Edité par CCSD ; Elsevier -

International audience. Here, we describe for the first time a Leishmania specific gene encoding a large 610 amino-acid RAB GTPase (LmLRAB). LmLRAB displays high homologies with the RAB GTPase protein family between amino acids 34 and 284. It contains characteristic signatures of RAB proteins: 4 GTP binding domains, 5 RAB specific domains, 3 RAB subfamily-specific domains, and a prenylation site. lmlrab is a single copy gene, transcribed as a 3.5 kb mRNA, highly conserved in Leishmania species, and encodes a protein doublet of approximately 75 kDa. Immunofluorescence microscopy using LmLRAB-specific antibodies demonstrated that LmLRAB is confined in a structure adjacent to the kinetoplast probably corresponding to an early endosomal/golgi apparatus localization. Interestingly, using quantitative real-time RT-PCR, we showed that the lmlrab gene is up-regulated twice in amastigotes relative to promastigotes. These findings suggest that LmLRAB may play a potential role in Leishmania pathogenicity.

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