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 journalArticlepeer-review

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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