title: Adhesion in Candida spp.
abstract: 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 epsilon 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.
authors.affiliation: Department of Molecular Virology, Immunology and Medical Genetics, The Ohio State University College of Medicine, Columbus, OH 43210-1239, USA. sundstrom.1@osu.edu
authors.forename: Paula
authors.initials: P
authors.lastname: Sundstrom
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002175:Candida / Q000235:genetics / Q000502:physiology*; D002177:Candidiasis / Q000378:metabolism; D002448:Cell Adhesion / Q000502:physiology*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016415:Sequence Alignment
chemical_list: D005656:Fungal Proteins