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Infection and Immunity, May 2004, p. 2780-2790, Vol. 72, No. 5
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.5.2780-2790.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Binding of Hematin by a New Class of Glutathione Transferase from the Blood-Feeding Parasitic Nematode Haemonchus contortus

Institute of Biological Sciences, University of Wales, Aberystwyth SY23 3DA,¹ Department of Veterinary Parasitology, University of Glasgow G61 1QH, United Kingdom,⁴ ID-Lelystad, 8200AB Lelystad, The Netherlands,² Victoria University of Wellington, Wellington 6001, New Zealand³

Received 17 December 2003/ Returned for modification 10 January 2004/ Accepted 22 January 2004

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.

Editor: W. A. Petri, Jr.

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