Show simple item record Strand, Mette Hoffmann, Karl F. 2011-01-04T15:26:28Z 2011-01-04T15:26:28Z 2011-01-04
dc.identifier.citation Strand , M & Hoffmann , K F 2011 , ' Molecular Characterization of a 20.8-kDa ' Schistosoma mansoni Antigen. The Journal of Biological Chemistry 272 (23) , pp. 14509 . en
dc.identifier.other PURE: 165278
dc.identifier.other dspace: 2160/6045
dc.description Hoffmann, K. F., Strand, M. (1997) Molecular Characterization of a 20.8-kDa Schistosoma mansoni Antigen. The Journal of Biological Chemistry 272 (23), pp. 14509¿14515 SEQUENCE SIMILARITY TO TEGUMENTAL ASSOCIATED ANTIGENS AND DYNEIN LIGHT CHAINS en
dc.description.abstract Survival of Schistosoma mansoni within the infected host requires the parasite to actively maintain its protective tegument. The components responsible for this maintenance are therefore attractive targets for immunoprophylaxis or chemotherapy. Here we report the molecular characterization of a 20.8-kDa tegumental antigen with sequence similarity to dynein light chains and tegumental associated antigens. A cDNA encoding the 20.8-kDa polypeptide contains an open reading frame of 181 amino acids and predicts an isoelectric point of 7.27. Expression of the 20.8-kDa antigen is developmentally regulated, with the highest concentration found in cercariae. Our data show that the 20.8-kDa polypeptide specifically interacts with a S. mansoni 10.4-kDa dynein light chain that we have previously described (Hoffmann, K. F., and Strand, M. (1996) J. Biol. Chem. 271, 26117¿26123). Velocity sedimentation analysis of a parasite extract demonstrated that this 10.4-kDa dynein light chain and the 20.8-kDa polypeptide were present in a complex that sedimented at 4.4 Svedberg units. We have also shown by antibody cross-reactivity that a 20.8- kDa homolog of the S. mansoni antigen is present in Schistosoma japonicum, but not in Schistosoma hematobium or Fasciola hepatica. Because the 20.8-kDa polypeptide displays ideal characteristics of a potential vaccine candidate, including (i) expression in the tegument, (ii) significant divergence from mammalian brain cytoplasmic dynein, and (iii) a conserved homolog in S. japonicum, we are currently evaluating its immunoprophylactic efficacy. en
dc.format.extent 14509 en
dc.language.iso eng
dc.relation.ispartof Schistosoma mansoni Antigen. The Journal of Biological Chemistry 272 (23) en
dc.title Molecular Characterization of a 20.8-kDa en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en

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