L-arginine availability and arginase activity: Characterization of amino acid permease 3 in Leishmania amazonensis.

ABSTRACT:

Background

Leishmania uses the amino acid L-arginine as a substrate for arginase, enzyme that produces urea and ornithine, last precursor of polyamine pathway. This pathway is used by the parasite to replicate and it is essential to establish the infection in the mammalian host. L-arginine is not synthesized by the parasite, so its uptake occurs through the amino acid permease 3 (AAP3). AAP3 is codified by two copies genes (5.1 and 4.7 copies), organized in tandem in the parasite genome. One copy presents the expression regulated by L-arginine availability.

Methodology/principal findings

RNA-seq data revealed 14 amino acid transporters differentially expressed in the comparison of La-WT vs. La-arg- promastigotes and axenic amastigotes. The 5.1 and 4.7 aap3 transcripts were d

SUBMITTER: Aoki JI 

PROVIDER: S-EPMC5693463 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature