Solution structure, membrane interactions, and protein binding partners of the tetraspanin Sm-TSP-2, a vaccine antigen from the human blood fluke schistosoma mansoni

Xinying Jia, Leigh Schulte, Alex Loukas, Darren Pickering, Mark Pearson, Mehdi Mobli, Alun Jones, Karl J. Rosengren, Norelle L. Daly, Geoffrey N. Gobert, Malcolm K. Jones, David J. Craik, Jason Mulvenna*

*Corresponding author for this work

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Background: Schistosome tetraspanin Sm-TSP-2 is a vaccine antigen.

Results: We describe the structure of the large extracellular domain of Sm-TSP-2, develop a model of its interactions with Tetraspanin-enriched-microdomain proteins and plasma membrane, and identify TEM constituents.

Conclusion: Structural conservation of the domain means this model is likely applicable to TSPs in general.

Significance: Tetraspanin-enriched-microdomain proteins provide further targets for multiplex vaccines and/or novel drug targets.
Original languageEnglish
Pages (from-to)7151-7163
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number10
Early online date15 Jan 2014
DOIs
Publication statusPublished - 07 Mar 2014
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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    Jia, X., Schulte, L., Loukas, A., Pickering, D., Pearson, M., Mobli, M., Jones, A., Rosengren, K. J., Daly, N. L., Gobert, G. N., Jones, M. K., Craik, D. J., & Mulvenna, J. (2014). Solution structure, membrane interactions, and protein binding partners of the tetraspanin Sm-TSP-2, a vaccine antigen from the human blood fluke schistosoma mansoni. Journal of Biological Chemistry, 289(10), 7151-7163. https://doi.org/10.1074/jbc.M113.531558