Adhesion in Candida spp

来自 EBSCO

阅读量:

50

作者:

P Sundstrom

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摘要:

Summary Microbial adherence is one of the most important determinants of pathogenesis, yet very few adhesins have been identified from fungal pathogens. Four structurally related adhesins, Hwp1, Ala1p/Als5p, Als1p, from Candida albicans and Epa1p from Candida glabrata , are members of a class of proteins termed glycosylphosphatidylinositol-dependent cell wall proteins (GPI-CWP). These proteins have N-terminal signal peptides and C-terminal features that mediate glycosylphosphatidylinositol (GPI) membrane anchor addition, as well as other determinants leading to attachment to cell wall glucan. While common signalP/GPI motifs facilitate cell surface expression, unique features mediate ligand binding specificities of adhesins. The first glimpse of structural features of putative adhesins has come from biophysical characterizations of the N-terminal domain of Als5p. One protein not in the GPI-CWP class that was initially described as an adhesin, Int1p, has recently been shown to be similar to Bud4p of Saccharomyces cerevisiae in primary amino acid sequence, in co-localizing with septins and in functioning in bud site selection. Progress in understanding the role of adhesins in oroesophageal candidiasis has been made for Hwp1 in a study using beige athymic and transgenic 26 mice that have combined defects in innate and acquired immune responses. Searches of the C. albicans genome for proteins in the GPI-CWP class has led to the identification of a subset of genes that will be the focus of future efforts to identify new Candida adhesins.

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DOI:

10.1046/j.1462-5822.2002.00206.x

被引量:

310

年份:

2010

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来源期刊

Cellular Microbiology
2010/5/14 0:00:00

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2010
被引量:59

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