Extracellular glycosylphosphatidylinositol-anchored mannoproteins and proteases ofCryptococcus neoformans

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Extracellular glycosylphosphatidylinositol-anchored mannoproteins and proteases of Cryptococcus neoformans.

Extracellular proteins of Cryptococcus neoformans are involved in the pathogenesis of cryptococcosis, and some are immunoreactive antigens that may potentially serve as candidates for vaccine development. To further study the extracellular proteome of the human fungal pathogen Cry. neoformans, we conducted a proteomic analysis of secreted and cell wall-bound proteins with an acapsular strain of...

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Biomedical applications of glycosylphosphatidylinositol-anchored proteins

Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) use a unique posttranslational modification to link proteins to lipid bilayer membranes. The anchoring structure consists of both a lipid and carbohydrate portion and is highly conserved in eukaryotic organisms regarding its basic characteristics, yet highly variable in its molecular details. The strong membrane targeting property h...

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Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins.

Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are a functionally and structurally diverse family of post-translationally modified membrane proteins found mostly in the outer leaflet of the plasma membrane in a variety of eukaryotic cells. Although the general role of GPI-APs remains unclear, they have attracted attention because they act as enzymes and receptors in cell adhesion, dif...

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Metabolism of glycosylphosphatidylinositol-anchored proteins in Arabidopsis.

Although glycosylphosphatidylinositol (GPI)-anchored proteins have now been found in several plants, very little is known regarding their metabolism there. This report describes studies of the biosynthesis and turnover of arabinogalactan proteins, a class of abundant GPI-anchored proteins secreted by cultured Arabidopsis cells.

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Glycosylphosphatidylinositol-anchored proteases of Candida albicans target proteins necessary for both cellular processes and host-pathogen interactions.

Intracellular and secreted proteases fulfill multiple functions in microorganisms. In pathogenic microorganisms extracellular proteases may be adapted to interactions with host cells. Here we describe two cell surface-associated aspartic proteases, Sap9 and Sap10, which have structural similarities to yapsins of Saccharomyces cerevisiae and are produced by the human pathogenic yeast Candida alb...

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ژورنال

عنوان ژورنال: FEMS Yeast Research

سال: 2007

ISSN: 1567-1356,1567-1364

DOI: 10.1111/j.1567-1364.2006.00198.x