Binding of hematin by a new class of glutathione transferase from the blood-feeding parasitic nematode Haemonchus contortus.
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.
van Rossum
Arjan J
AJ
Institute of Biological Sciences, University of Wales, Aberystwyth SY23 3DA, United Kingdom. ajv@aber.ac.uk
Jefferies
James R
JR
Rijsewijk
Frans A M
FA
LaCourse
E James
EJ
Teesdale-Spittle
Paul
P
Barrett
John
J
Tait
Andrew
A
Brophy
Peter M
PM
D000818:Animals; D015153:Blotting, Western; D015180:Electrophoresis, Gel, Two-Dimensional; D005982:Glutathione Transferase / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D006189:Haemonchus / Q000201:enzymology* / Q000235:genetics; D006427:Hemin / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D011994:Recombinant Proteins; D006427:Hemin; D005982:Glutathione Transferase