ll Biological Characterization of the Malaria Vaccine ndidate Trophozoite Exported Protein 1.
- Resource Type
- Article
- Authors
- Kulangara, Caroline; Luedin, Samuel; Dietz, Olivier; Rusch, Sebastian; Frank, Geraldine; Mueller, Dania; Moser, Mirjam; Kajava, Andrey V.; Corradin, Giampietro; Beck, Hans-Peter; Felger, Ingrid
- Source
- PLoS ONE. Oct2012, Vol. 7 Issue 10, Special section p1-10. 10p.
- Subject
- *GENOMICS
*VACCINES
*PROTEINS
*TROPHOZOITES
*PEPTIDES
*MALARIA vaccines
- Language
- ISSN
- 1932-6203
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. [ABSTRACT FROM AUTHOR]