Biochemical characterization and vaccine potential of a heme-binding glutathione transferase from the adult hookworm Ancylostoma caninum

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dc.contributor.author Zhan, Bin
dc.contributor.author Liu, Sen
dc.contributor.author Perally, Samirah
dc.contributor.author Xue, Jian
dc.contributor.author Fujiwara, Ricardo
dc.contributor.author Brophy, Peter Michael
dc.contributor.author Xiao, Shuhua
dc.contributor.author Liu, Yueyuan
dc.contributor.author Feng, Jianjun
dc.contributor.author Williamson, Angela
dc.contributor.author Wang, Yan
dc.contributor.author Bueno, Lilian L.
dc.contributor.author Mendez, Susana
dc.contributor.author Goud, Gaddam
dc.contributor.author Bethony, Jeffrey M.
dc.contributor.author Hawdon, John M.
dc.contributor.author Loukas, Alex
dc.contributor.author Jones, Karen
dc.contributor.author Hotez, Peter J.
dc.date.accessioned 2009-09-02T13:10:09Z
dc.date.available 2009-09-02T13:10:09Z
dc.date.issued 2005-10
dc.identifier.citation Zhan , B , Liu , S , Perally , S , Xue , J , Fujiwara , R , Brophy , P M , Xiao , S , Liu , Y , Feng , J , Williamson , A , Wang , Y , Bueno , L L , Mendez , S , Goud , G , Bethony , J M , Hawdon , J M , Loukas , A , Jones , K & Hotez , P J 2005 , ' Biochemical characterization and vaccine potential of a heme-binding glutathione transferase from the adult hookworm Ancylostoma caninum ' Infection and Immunity , vol 73 , no. 10 , pp. 6903-6911 . en
dc.identifier.issn 0019-9567
dc.identifier.other PURE: 116470
dc.identifier.other dspace: 2160/2881
dc.identifier.uri http://hdl.handle.net/2160/2881
dc.description Zhan, B., Liu, S., Perally, S., Xue, J., Fujiwara, R., Brophy, P., Xiao, S. H., Liu, Y. Y., Feng, J. J., Williamson, A., Wang, Y., Bueno, L. L., Mendez, S., Goud, G., Bethony, J. M., Hawdon, J. M., Loukas, A., Jones, K., Hotez, P. J. (2005). Biochemical characterization and vaccine potential of a heme-binding glutathione transferase from the adult hookworm Ancylostoma caninum.   Infection and Immunity, 73, (10), 6903-6911. Sponsorship: Human Hookworm Vaccine Initiative of the Sabin Vaccine Institute / Bill and Melinda Gates Foundation. / BBSRC en
dc.description.abstract We report the cloning and expression of Ac-GST-1, a novel glutathione S-transferase from the adult hookworm Ancylostoma caninum, and its possible role in parasite blood feeding and as a vaccine target. The predicted Ac-GST-1 open reading frame contains 207 amino acids (mass, 24 kDa) and exhibited up to 65% amino acid identity with other nematode GSTs. mRNA encoding Ac-GST-1 was detected in adults, eggs, and larval stages, but the protein was detected only in adult hookworm somatic extracts and excretory/secretory products. Using antiserum to the recombinant protein, Ac-GST-1 was immunolocalized to the parasite hypodermis and muscle tissue and weakly to the intestine. Recombinant Ac-GST-1 was enzymatically active, as determined by conjugation of glutathione to a model substrate, and exhibited a novel high-affinity binding site for hematin. The possible role of Ac-GST-1 in parasite heme detoxification during hemoglobin digestion or heme uptake prompted interest in evaluating it as a potential vaccine antigen. Vaccination of dogs with Ac-GST-1 resulted in a 39.4% reduction in the mean worm burden and 32.3% reduction in egg counts compared to control dogs following larval challenge, although the reductions were not statistically significant. However, hamsters vaccinated with Ac-GST-1 exhibited statistically significant worm reduction (53.7%) following challenge with heterologous Necator americanus larvae. These studies suggest that Ac-GST-1 is a possible drug and vaccine target for hookworm infection. en
dc.format.extent 9 en
dc.language.iso eng
dc.relation.ispartof Infection and Immunity en
dc.title Biochemical characterization and vaccine potential of a heme-binding glutathione transferase from the adult hookworm Ancylostoma caninum en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1128/IAI.73.10.6903-6911.2005
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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