Binding of hematin to a new class of glutathione transferase from the blood-feeding parasitic nematode Haemonchus contortus.

Peter M. Brophy, James R. Jefferies, Paul Teesdale-Spittle, Andrew Tait, Arjan Johannes van Rossum, E. James LaCourse, Frans A. M. Rijsewijk, John Barrett

Research output: Contribution to journalArticlepeer-review

45 Citations (SciVal)

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
Number of pages11
JournalInfection and Immunity
DOIs
Publication statusPublished - May 2004

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