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Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major
Published on: October 28, 2022
Characterization of two different mucolipin-like genes from Leishmania major
Mehdi Chenik1, Feriel Douagi, Yosser Ben Achour
1Laboratoire d'Immunopathologie, Vaccinologie et Génétique Moléculaire, Institut Pasteur de Tunis, 13, Place Pasteur, 1002, Tunis-Belvédère, Tunisia. mehdi.chenik@pasteur.rns.tn
Abstract:
Here, we report the existence of two different mucolipin-like genes in Leishmania parasites. The Leishmania major mucolipin-like A and B genes (lmmlA and lmmlB) encode two proteins of 776 and 590 amino acids, respectively, and may be classified among the mucolipins family [transient receptors potential mucolipin (TRPML)] because (1) they include a large region that exhibits significant similarities with specific domains of ion transport proteins and transient receptors potential (TRP) channels, (2) they contain at least 173 residues that display significant homologies with conserved regions of different mucolipins from several species, and (3) as TRPMLs, they include six predicted transmembrane domains. Gene expression analysis reveals that lmmlB is upregulated in metacyclics and amastigotes relative to procyclics, while lmmlA is constitutively expressed in the three Leishmania developmental stages. These genes could constitute potential drug targets.
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