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Cloning and characterization of glutamate dehydrogenase (GDH) from the gut of Haemonchus contortus

Published online by Cambridge University Press:  01 March 1999

P. J. SKUCE ,
E. M. STEWART ,
W. D. SMITH  and
D. P. KNOX
P. J. SKUCE
Affiliation:
Moredun Research Institute, International Research Centre, Pentlands Science Park, Bush Loan, Penicuik, Midlothian EH26 0PZ, UK
E. M. STEWART
Affiliation:
Moredun Research Institute, International Research Centre, Pentlands Science Park, Bush Loan, Penicuik, Midlothian EH26 0PZ, UK
W. D. SMITH
Affiliation:
Moredun Research Institute, International Research Centre, Pentlands Science Park, Bush Loan, Penicuik, Midlothian EH26 0PZ, UK
D. P. KNOX
Affiliation:
Moredun Research Institute, International Research Centre, Pentlands Science Park, Bush Loan, Penicuik, Midlothian EH26 0PZ, UK
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Abstract

Vaccination of lambs with the membrane-bound (S3) thiol-Sepharose binding protein (TSBP) fraction derived from the gut of Haemonchus contortus confers significant protection against homologous challenge. The S3 TSBP peptide profile is dominated by a major protein of ca. 60 kDa which is strongly recognized by antisera from sheep demonstrably protected following immunization with S3 TSBP. In an attempt to identify this protein, sera from protected lambs were employed to screen a λgt11 cDNA library of the adult parasite and resulted in the isolation of numerous clones encoding a homologue of the mitochondrial enzyme, glutamate dehydrogenase (GDH). GDH enzyme activity was readily demonstrable in S3 TSBP material and immunolocalization studies showed that the enzyme was localized to the cytoplasm of the parasite's gut. Furthermore, the enzyme appeared to be developmentally regulated, with both GDH mRNA and protein expressed almost exclusively during the blood-feeding parasitic stages.

Keywords

Haemonchus contortusvaccinationthiol-binding proteinsglutamate dehydrogenasepolymerase chain reaction
Type
Research Article
Information
Parasitology , Volume 118 , Issue 3 , March 1999 , pp. 297 - 304
Copyright
1999 Cambridge University Press

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Footnotes

Note: Nucleotide sequence data reported in this paper are available in the GenBank data base under the accession number AF000967.