Molecular Cloning, Biochemical Characterization, and Partial Protective Immunity of the Heme-Binding Glutathione S-Transferases from the Human Hookworm Necator americanus

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dc.contributor.author Zhan, Bin
dc.contributor.author Perally, Samirah
dc.contributor.author Brophy, Peter M.
dc.contributor.author Xue, Jian
dc.contributor.author Goud, Gaddam
dc.contributor.author Liu, Sen
dc.contributor.author Deumic, Vehid
dc.contributor.author de Oliveira, Luciana
dc.contributor.author Bethony, Jeffrey
dc.contributor.author Bottazzi, Maria Elena
dc.contributor.author Jiang, Desheng
dc.contributor.author Gillespie, Portia
dc.contributor.author Xiao, Shu-hua
dc.contributor.author Gupta, Richi
dc.contributor.author Loukas, Alex
dc.contributor.author Ranjit, Najju
dc.contributor.author Lustigman, Sara
dc.contributor.author Hotez, Peter
dc.contributor.author Oksov, Yelena
dc.date.accessioned 2011-06-09T09:01:45Z
dc.date.available 2011-06-09T09:01:45Z
dc.date.issued 2010-04
dc.identifier.citation Zhan , B , Perally , S , Brophy , P M , Xue , J , Goud , G , Liu , S , Deumic , V , de Oliveira , L , Bethony , J , Bottazzi , M E , Jiang , D , Gillespie , P , Xiao , S , Gupta , R , Loukas , A , Ranjit , N , Lustigman , S , Hotez , P & Oksov , Y 2010 , ' Molecular Cloning, Biochemical Characterization, and Partial Protective Immunity of the Heme-Binding Glutathione S-Transferases from the Human Hookworm Necator americanus ' Infection and Immunity , vol 78 , no. 4 , pp. 1552-1563 . , 10.1128/IAI.00848-09 en
dc.identifier.issn 0019-9567
dc.identifier.other PURE: 164215
dc.identifier.other dspace: 2160/7016
dc.identifier.uri http://hdl.handle.net/2160/7016
dc.identifier.uri http://iai.asm.org/cgi/reprint/IAI.00848-09v1 en
dc.description Zhan, B., Perally, S., Brophy, P. M., Xue, J., Goud, G., Liu, S., Deumic, V., de Oliveira, L., Bethony, J., Bottazzi, M. E., Jiang, D., Gillespie, P., Xiao, S., Gupta, R., Loukas, A., Ranjit, N., Lustigman, S., Hotez, P. (2010). Molecular cloning, biochemical characterization, and partial protective immunity of the heme-binding glutathione transferases from the human hookworm Necator americanus. Infection and Immunity, 78 (4), 1552-1563. IMPF: 04.09 en
dc.description.abstract Hookworm glutathione S-transferases (GSTs) are critical for parasite blood feeding and survival and represent potential targets for vaccination. Three cDNAs, each encoding a full-length GST protein from the human hookworm Necator americanus (and designated Na-GST-1, Na-GST-2, and Na-GST-3, respectively) were isolated from cDNA based on their sequence similarity to Ac-GST-1, a GST from the dog hookworm Ancylostoma caninum. The open reading frames of the three N. americanus GSTs each contain 206 amino acids with 51% to 69% sequence identity between each other and Ac-GST-1. Sequence alignment with GSTs from other organisms shows that the three Na-GSTs belong to a nematode-specific nu-class GST family. All three Na-GSTs, when expressed in Pichia pastoris, exhibited low lipid peroxidase and glutathione-conjugating enzymatic activities but high heme-binding capacities, and they may be involved in the detoxification and/or transport of heme. In two separate vaccine trials, recombinant Na-GST-1 formulated with Alhydrogel elicited 32 and 39% reductions in adult hookworm burdens (P < 0.05) following N. americanus larval challenge relative to the results for a group immunized with Alhydrogel alone. In contrast, no protection was observed in vaccine trials with Na-GST-2 or Na-GST-3. On the basis of these and other preclinical data, Na-GST-1 is under possible consideration for further vaccine development. en
dc.format.extent 12 en
dc.language.iso eng
dc.relation.ispartof Infection and Immunity en
dc.title Molecular Cloning, Biochemical Characterization, and Partial Protective Immunity of the Heme-Binding Glutathione S-Transferases from the Human Hookworm Necator americanus en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1128/IAI.00848-09
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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