title: The expression of HSP83 genes in Leishmania infantum is affected by temperature and by stage-differentiation and is regulated at the levels of mRNA stability and translation.
abstract: BACKGROUND
  Exposure of Leishmania promastigotes to the temperature of their mammalian hosts results in the induction of a typical heat shock response. It has been suggested that heat shock proteins play an important role in parasite survival and differentiation.
  
  
  RESULTS
  Here we report the studies on the expression of the heat shock protein 83 (HSP83) genes of Leishmania infantum. Confirming previous observations for other Leishmania species, we found that the L. infantum HSP83 transcripts also show a temperature-dependent accumulation that is controlled by a post-transcriptional mechanism involving sequences located in the 3'-untranslated region (3'-UTR). However, contrary to that described for L. amazonensis, the accumulation of the HSP83 transcripts in L. infantum is dependent on active protein synthesis. The translation of HSP83 transcripts is enhanced during heat shock and, as first described in L. amazonensis, we show that the 3'-UTR of the L. infantum HSP83 gene is essential for this translational control. Measurement of the steady-state levels of HSP83 transcripts along the promastigote-to-amastigote differentiation evidenced a specific profile of HSP83 RNAs: after an initial accumulation of HSP83 transcripts observed short after (2 h) incubation in the differentiation conditions, the amount of HSP83 RNA decreased to a steady-state level lower than in undifferentiated promastigotes. We show that this transient accumulation is linked to the presence of the 3'-UTR and flanking regions. Again, an 8-fold increase in translation of the HSP83 transcripts is observed short after the initiation of the axenic differentiation, but it is not sustained after 9 h.
  
  
  CONCLUSIONS
  This transient expression of HSP83 genes could be relevant for the differentiation of Leishmania, and the underlying regulatory mechanism may be part of the developmental program of this parasite.
authors.affiliation: Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, 28049, Spain. rlarreta@cbm.uam.es
authors.forename: Ruth
authors.initials: R
authors.lastname: Larreta
authors.forename: Manuel
authors.initials: M
authors.lastname: Soto
authors.forename: Luis
authors.initials: L
authors.lastname: Quijada
authors.forename: Cristina
authors.initials: C
authors.lastname: Folgueira
authors.forename: Daniel R
authors.initials: DR
authors.lastname: Abanades
authors.forename: Carlos
authors.initials: C
authors.lastname: Alonso
authors.forename: Jose M
authors.initials: JM
authors.lastname: Requena
mesh_terms: D020413:3' Untranslated Regions / Q000235:genetics / Q000502:physiology; D000818:Animals; D002454:Cell Differentiation / Q000502:physiology*; D016054:DNA, Protozoan / Q000235:genetics / Q000502:physiology; D018507:Gene Expression Regulation, Developmental / Q000502:physiology*; D017930:Genes, Reporter / Q000502:physiology; D006360:Heat-Shock Proteins / Q000235:genetics*; D018314:Leishmania infantum / Q000235:genetics*; D014176:Protein Biosynthesis / Q000502:physiology*; D015800:Protozoan Proteins / Q000235:genetics; D020871:RNA Stability / Q000502:physiology*; D012333:RNA, Messenger / Q000378:metabolism; D013696:Temperature
chemical_list: D020413:3' Untranslated Regions; D016054:DNA, Protozoan; D006360:Heat-Shock Proteins; C490310:Hsp83 protein, protozoan; D015800:Protozoan Proteins; D012333:RNA, Messenger