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- W1569112746 abstract "The Candida genus is a polyphyletic genus with at least 150 species. Nine are recognized opportunistic pathogens of humans and animals. C. albicans is the species most frequently isolated from human infections, followed by Candida non-Candida species (CNCA), as C. glabrata, C. tropicalis, C. dubliniensis, C. parapsilosis, C. guilliermondii, C. lusitaniae, C. kefyr and C. krusei (Mean et al. 2008; Pfaller & Diekema, 2007; Almirante et al. 2005; Manzano-Gayosso et al. 2000). Some works describe the phylogenetic relationships of Candida genus and illustrate the limited relationship between the pathogenic Candida spp. The genus has been divided into: the CTG clade, which includes yeast that encodes CTG as serine instead of leucine (C. albicans, C. dubliniensis, C. tropicalis, C. parapsilosis and C. lusitaniae); and the WGD clade, which includes yeast that has undergone a genome duplication event (Saccharomyces spp., Kluyveromyces spp. and C. glabrata). Evidently, C. glabrata is more related to non-pathogenic yeasts, as Saccharomyces cerevisiae, than to the other pathogenic species (Scannell et al. 2007). C. albicans is a normal microorganism in humans, and colonise up to 70% of skin, mucoses, and faeces of individuals with no apparent detriment to health. However, in some circumstances, either through environmental factors or a weakening of the host immune system, a proliferation and infection by C. albicans arise inducing candidosis (Wei et al. 2011). Biofilm formation, adhesion, cavitation, phenotypic switching, dimorphism, interaction with the host immune system, invasion and tissue damage are virulence virulence factors for C. albicans. All these factors are related to the secreted aspartyl proteases (Sap) family, which is considered an important virulence factor and is studied as a possible target for therapeutic drug design (Naglik et al. 2004; Chaffin et al. 1998; Hube, 1998; Naglik et al. 2003, 2004, 2008). The topic of this chapter is to understand the molecular characteristics, evolution and putative functions of glycosylphosphatidylinositol (GPI)-linked aspartyl proteases (Yps), a protein superfamily distributed among all pathogenic Candida species. Cell location motifs," @default.
- W1569112746 created "2016-06-24" @default.
- W1569112746 creator A5042156744 @default.
- W1569112746 creator A5049596179 @default.
- W1569112746 creator A5089040635 @default.
- W1569112746 date "2011-10-17" @default.
- W1569112746 modified "2023-10-17" @default.
- W1569112746 title "Evolution of GPI-Aspartyl Proteinases (Yapsines) of Candida spp" @default.
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