A novel phospholipase from Trypanosoma brucei

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25 Citations (Scopus)

Abstract

Phospholipase A(1) activities have been detected in most cells where they have been sought and yet their characterization lags far behind that of the phospholipases A(2), C and D. The study presented here details the first cloning and characterization of a cytosolic PLA(1) that exhibits preference for phosphatidylcholine (GPCho) substrates. Trypanosoma brucei phospholipase A(1) (TbPLA(1)) is unique from previously identified eukaryotic PLA(1) because it is evolutionarily related to bacterial secreted PLA(1). A T. brucei ancestor most likely acquired the PLA(1) from a horizontal gene transfer of a PLA(1) from Sodalis glossinidius, a bacterial endosymbiont of tsetse flies. Nano-electrospray ionization tandem mass spectrometry analysis of TbPLA(1) mutants established that the enzyme functions in vivo to synthesize lysoGPCho metabolites containing long-chain mostly polyunsaturated and highly unsaturated fatty acids. Analysis of purified mutated recombinant forms of TbPLA(1) revealed that this enzyme is a serine hydrolase whose catalytic mechanism involves a triad consisting of the amino acid residues Ser-131, His-234 and Asp-183. The TbPLA(1) homozygous null mutants generated here constitute the only PLA(1) double knockouts from any organism.

Original languageEnglish
Pages (from-to)1078-1095
Number of pages18
JournalMolecular Microbiology
Volume63
Issue number4
DOIs
Publication statusPublished - Feb 2007

Keywords

  • MAMMALIAN SEC23P-INTERACTING PROTEIN
  • LATERAL GENE-TRANSFER
  • ARACHIDONIC-ACID
  • BLOOD-STREAM
  • FATTY-ACIDS
  • BOVINE BRAIN
  • GUINEA-PIG
  • AFRICAN TRYPANOSOMES
  • SEQUENCE SIMILARITY
  • ESCHERICHIA-COLI

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