Differential expression of glutathione S-transferase (GST) by adult Heligmosomoides polygyrus during primary infection in fast and slow responding hosts.
Glutathione S-transferase (GST) specific enzymatic activity, assayed with the model substrate 1-chloro-2,4-dinitrobenzene, was 45% higher in adult Heligmosomoides polygyrus passaged through a slow responder mouse strain, C57/BL10 compared to worms passaged through a fast-responder strain (SWR x SJL) F1. Western analysis using polyclonal antisera raised to purified H. polygyrus GSTs did not appear to positively correlate the expression of GST protein with functional enzymatic activity. However, western blotting did indicate a sex-linked expression pattern of GST protein, with male worms expressing a higher ratio of the 24 kDa to the 23 kDa GST family than female worms.
Brophy
P M
PM
Department of Pharmaceutical Sciences, School of Applied Sciences, De Montfort University, Leicester, U.K.
Ben-Smith
A
A
Brown
A
A
Behnke
J M
JM
Pritchard
D I
DI
D000818:Animals; D000909:Antibodies, Helminth; D015153:Blotting, Western; D004137:Dinitrochlorobenzene; D005260:Female; D005982:Glutathione Transferase / Q000096:biosynthesis / Q000378:metabolism*; D006790:Host-Parasite Interactions; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009351:Nematospiroides dubius / Q000201:enzymology*; D012727:Sex Characteristics; D017206:Strongylida Infections / Q000469:parasitology*
D000909:Antibodies, Helminth; D004137:Dinitrochlorobenzene; D005982:Glutathione Transferase