Binding of hematin by a nem class of glutathione transferase from the blood-feeding parasitic nematode Haemonchus contortus

A.J. Rossum, J.R. Jefferies, F.A.M. Rijsewijk, E.J. LaCourse, P. Teesdale, J. Barrett, A. Tait, P.M. Brophy

    Research output: Contribution to journalArticleAcademicpeer-review

    42 Citations (Scopus)

    Abstract

    The phase II detoxification system glutathione transferase (GST) is associated with the establishment of parasitic nematode infections within the gastrointestinal environment of the mammalian host. We report the functional analysis of a GST from an important worldwide parasitic nematode of small ruminants, Haemonchus contortus. This GST shows limited activity with a range of classical GST substrates but effectively binds hematin. The high-affinity binding site for hematin was not present in the GST showing the most identity, CE07055 from the free-living nematode Caenorhabditis elegans. This finding suggests that the high-affinity binding of hematin may represent a parasite adaptation to blood or tissue feeding from the host.
    Original languageEnglish
    Pages (from-to)2780-2790
    JournalInfection and Immunity
    Volume72
    Issue number5
    DOIs
    Publication statusPublished - 2004

    Keywords

    • tapeworm moniezia-expansa
    • s-transferases
    • heligmosomoides-polygyrus
    • lipid-peroxidation
    • anthelmintic resistance
    • necator-americanus
    • protein
    • expression
    • products
    • identification

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