alexa Binding of hematin by a new class of glutathione transferase from the blood-feeding parasitic nematode Haemonchus contortus.
Bioinformatics & Systems Biology

Bioinformatics & Systems Biology

Metabolomics:Open Access

Author(s): van Rossum AJ, Jefferies JR, Rijsewijk FA, LaCourse EJ, TeesdaleSpittle P,

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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.
This article was published in Infect Immun and referenced in Metabolomics:Open Access

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