Screening for glycosylphosphatidylinositol-anchored proteins in the Paracoccidioides brasiliensis transcriptome
Genet. mol. res. (Online)
;
4(2): 326-345, 30 jun. 2005. tab, ilus
Artículo
en Inglés
| LILACS
| ID: lil-445284
ABSTRACT
Open reading frames in the transcriptome of Paracoccidioides brasiliensis were screened for potential glycosylphosphatidylinositol (GPI)-anchored proteins, which are a functionally and structurally diverse family of post-translationally modified molecules found in a variety of eukaryotic cells. Numerous studies have demonstrated that various GPI anchor sequences can affect the localization of these proteins in the plasma membrane or the cell wall. The GPI anchor core is produced in the endoplasmic reticulum by sequential addition of monosaccharides and phospho-ethanolamine to phosphatidylinositol. The complete GPI anchor is post-translationally attached to the protein carboxyl-terminus by GPI transamidases. Removal of this GPI lipid moiety by phospholipases generates a soluble form of the protein. The identification of putative GPI-attached proteins in the P. brasiliensis transcriptome was based on the following criteria the presence of an N-terminal signal peptide for secretion and a hydrophobic region in the C-terminus presenting the GPI-attachment site. The proteins that were identified were in several functional categories i) eight proteins were predicted to be enzymes (Gel1, Gel2, Gel3, alpha-amylase, aspartic proteinase, Cu-Zn SOD, DFG5, PLB); ii) Ag2/PRA, ELI-Ag1 and Gel1 are probably surface antigens; iii) Crh-like and the GPI-anchored cell wall protein have a putative structural role; iv) ECM33 and Gels (1, 2 and 3) are possibly involved in cell wall biosynthesis, and v) extracellular matrix protein is considered to be an adhesion protein. In addition, eight deduced proteins were predicted to localize in the plasma membrane and six in the cell wall. We also identified proteins involved in the synthesis, attachment and cleaving of the GPI anchor in the P. brasiliensis transcriptome.
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LILACS (Américas)
Asunto principal:
Paracoccidioides
/
Pared Celular
/
Sistemas de Lectura Abierta
/
Glicosilfosfatidilinositoles
/
Proteínas de la Membrana
Tipo de estudio:
Estudio diagnóstico
/
Estudio pronóstico
/
Estudio de tamizaje
Límite:
Humanos
País/Región como asunto:
America del Sur
/
Brasil
Idioma:
Inglés
Revista:
Genet. mol. res. (Online)
Asunto de la revista:
Biologia Molecular
/
Genética
Año:
2005
Tipo del documento:
Artículo
País de afiliación:
Brasil
Institución/País de afiliación:
Universidade Federal de Goiás/BR
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