Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
Data(s) |
2012
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Resumo |
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. |
Identificador |
http://serval.unil.ch/?id=serval:BIB_26E975D339E7 isbn:1932-6203 (Electronic) pmid:23056243 doi:10.1371/journal.pone.0046112 isiid:000309831500027 |
Idioma(s) |
en |
Fonte |
Plos One, vol. 7, no. 10, pp. e46112 |
Tipo |
info:eu-repo/semantics/article article |