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Literature summary extracted from

  • Singh, K.; Ali, V.; Pratap Singh, K.; Gupta, P.; Suman, S.S.; Ghosh, A.K.; Bimal, S.; Pandey, K.; Das, P.
    Deciphering the interplay between cysteine synthase and thiol cascade proteins in modulating Amphotericin B resistance and survival of Leishmania donovani under oxidative stress (2017), Redox Biol., 12, 350-366 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.47 Leishmania donovani G1C2I2
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General Information

EC Number General Information Comment Organism
2.5.1.47 physiological function overexpression of cysteine synthase in amphotericin B (Amp B) sensitive strain S1-OE modulates resistance towards oxidative stress and drug pressure. Antioxidant enzyme activities are upregulated in S1-OE parasites and these parasites alleviate intracellular reactive oxygen species efficiently by maintaining the reduced thiol pool. The Amp B sensitive strain shows higher levels of reactive oxygen species which is positively correlated with the protein carbonylation levels and negatively correlated with cell viability. Cysteine synthase overexpression also augments the ROS-primed induction of cysteine synthase-GFP as well as endogenous cysteine synthase and thiol pathway proteins in Leishmania donovani parasites. The expression of cysteine synthase is upregulated in Amp B resistant isolates and during infective stationary stages of growth. Cysteine synthase overexpression enhances the infectivity of Leishmania donovani parasites Leishmania donovani