Oct 12, 2012

Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1

PloS One
C KulangaraIngrid Felger

Abstract

In a genome-wide screen for alpha-helical coiled coil motifs aiming at structurally defined vaccine candidates we identified PFF0165c. This protein is exported in the trophozoite stage and was named accordingly Trophozoite exported protein 1 (Tex1). In an extensive preclinical evaluation of its coiled coil peptides Tex1 was identified as promising novel malaria vaccine candidate providing the rational for a comprehensive cell biological characterization of Tex1. Antibodies generated against an intrinsically unstructured N-terminal region of Tex1 and against a coiled coil domain were used to investigate cytological localization, solubility and expression profile. Co-localization experiments revealed that Tex1 is exported across the parasitophorous vacuole membrane and located to Maurer's clefts. Change in location is accompanied by a change in solubility: from a soluble state within the parasite to a membrane-associated state after export to Maurer's clefts. No classical export motifs such as PEXEL, signal sequence/anchor or transmembrane domain was identified for Tex1.

  • References39
  • Citations7

Mentioned in this Paper

Pathologic Cytolysis
Thaw
REXO1 gene
Establishment and Maintenance of Localization
Saponin
Real-Time Polymerase Chain Reaction
Monoclonal Antibodies
Monoclonal antibodies, antineoplastic
Protease Inhibitors [MoA]
Ethanol

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