What has proteomics taught us about Leishmania development?
- PMID: 22369930
- DOI: 10.1017/S0031182012000157
What has proteomics taught us about Leishmania development?
Abstract
Leishmania are obligatory intracellular parasitic protozoa that cycle between sand fly mid-gut and phagolysosomes of mammalian macrophages. They have developed genetically programmed changes in gene and protein expression that enable rapid optimization of cell function according to vector and host environments. During the last two decades, host-free systems that mimic intra-lysosomal environments have been devised in which promastigotes differentiate into amastigotes axenically. These cultures have facilitated detailed investigation of the molecular mechanisms underlying Leishmania development inside its host. Axenic promastigotes and amastigotes have been subjected to transcriptome and proteomic analyses. Development had appeared somewhat variable but was revealed by proteomics to be strictly coordinated and regulated. Here we summarize the current understanding of Leishmania promastigote to amastigote differentiation, highlighting the data generated by proteomics.
Similar articles
-
Identification of developmentally-regulated proteins in Leishmania panamensis by proteome profiling of promastigotes and axenic amastigotes.Mol Biochem Parasitol. 2006 May;147(1):64-73. doi: 10.1016/j.molbiopara.2006.01.008. Epub 2006 Feb 9. Mol Biochem Parasitol. 2006. PMID: 16530278
-
Phosphoproteomic analysis of differentiating Leishmania parasites reveals a unique stage-specific phosphorylation motif.J Proteome Res. 2013 Jul 5;12(7):3405-12. doi: 10.1021/pr4002492. Epub 2013 Jun 11. J Proteome Res. 2013. PMID: 23688256
-
Phlebotomine sand flies and Leishmania parasites: friends or foes?Trends Parasitol. 2006 Sep;22(9):439-45. doi: 10.1016/j.pt.2006.06.012. Epub 2006 Jul 14. Trends Parasitol. 2006. PMID: 16843727 Review.
-
Genomic and proteomic expression analysis of Leishmania promastigote and amastigote life stages: the Leishmania genome is constitutively expressed.Mol Biochem Parasitol. 2007 Mar;152(1):35-46. doi: 10.1016/j.molbiopara.2006.11.009. Epub 2006 Dec 8. Mol Biochem Parasitol. 2007. PMID: 17188763
-
Global gene expression in Leishmania.Int J Parasitol. 2007 Aug;37(10):1077-86. doi: 10.1016/j.ijpara.2007.04.011. Epub 2007 May 6. Int J Parasitol. 2007. PMID: 17574557 Review.
Cited by
-
Quantitative single-cell analysis of Leishmania major amastigote differentiation demonstrates variably extended expression of the lipophosphoglycan (LPG) virulence factor in different host cell types.PLoS Negl Trop Dis. 2022 Oct 27;16(10):e0010893. doi: 10.1371/journal.pntd.0010893. eCollection 2022 Oct. PLoS Negl Trop Dis. 2022. PMID: 36302046 Free PMC article.
-
Ascorbate-Dependent Peroxidase (APX) from Leishmania amazonensis Is a Reactive Oxygen Species-Induced Essential Enzyme That Regulates Virulence.Infect Immun. 2019 Nov 18;87(12):e00193-19. doi: 10.1128/IAI.00193-19. Print 2019 Dec. Infect Immun. 2019. PMID: 31527128 Free PMC article.
-
Discovery of novel hit compounds with broad activity against visceral and cutaneous Leishmania species by comparative phenotypic screening.Sci Rep. 2019 Jan 24;9(1):438. doi: 10.1038/s41598-018-36944-6. Sci Rep. 2019. PMID: 30679614 Free PMC article.
-
Characterisation of a putative glutamate 5-kinase from Leishmania donovani.FEBS J. 2018 Jul;285(14):2662-2678. doi: 10.1111/febs.14511. Epub 2018 May 27. FEBS J. 2018. PMID: 29777624 Free PMC article.
-
The iron-dependent mitochondrial superoxide dismutase SODA promotes Leishmania virulence.J Biol Chem. 2017 Jul 21;292(29):12324-12338. doi: 10.1074/jbc.M116.772624. Epub 2017 May 26. J Biol Chem. 2017. PMID: 28550086 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Medical
