Molecular bases of adhesion of<i>Candida albicans</i>

Yoshimura, Fuminobu; Kagaya, Keiko

doi:10.1080/02681219780000971

Cited by 107 publications

(74 citation statements)

References 89 publications

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“…Cell-cell adhesion and recognition in A. areolatum further appear to be lectin-mediated, because the two glycoprotein-encoding ESTs identified in this study encode a putative mucin and a mannoprotein. By functioning as lectins, these proteins are thought to facilitate cell-cell adhesion by binding to cell surface carbohydrates in fungi (Fukazawa and Kagaya, 1997;Fichtner et al, 2007;Douglas et al, 2007). The fact that transcripts for both these proteins were up-regulated during vegetative compatibility and incompatibility relative to non-interacting mycelia, supports the notion that similar molecular mechanisms underlie hyphal fusion during these interactions.…”

Section: Discussionsupporting

confidence: 59%

Gene expression associated with vegetative incompatibility in Amylostereum areolatum

Nest¹,

Steenkamp²,

Slippers³

et al. 2011

Fungal Genetics and Biology

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In filamentous fungi, vegetative compatibility among individuals of the same species is determined by the genes encoded at the heterokaryon incompatibility (het) loci. The hyphae of genetically similar individuals that share the same allelic specificities at their het loci are able to fuse and intermingle, while different allelic specificities at the het loci result in cell death of the interacting hyphae. In this study, suppression subtractive hybridization (SSH) followed by pyrosequencing and quantitative reverse transcription PCR were used to identify genes that are selectively expressed when vegetatively incompatible individuals of Amylostereum areolatum interact. The SSH library contained genes associated with various cellular processes, including cell-cell adhesion, stress and defence responses, as well as cell death. Some of the transcripts encoded proteins that were previously implicated in the stress and defence responses associated with vegetative incompatibility. Other transcripts encoded proteins known to be associated with programmed cell death, but have not previously been linked with vegetative incompatibility.Results of this study have considerably increased our knowledge of the processes underlying vegetative incompatibility in Basidiomycetes in general and A. areolatum in particular.

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Section: Discussionsupporting

confidence: 59%

Gene expression associated with vegetative incompatibility in Amylostereum areolatum

Nest¹,

Steenkamp²,

Slippers³

et al. 2011

Fungal Genetics and Biology

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“…The highly glycosylated mannoproteins play important roles in adhesion, antigenicity, and modulation of the host immune responses (7)(8)(9)(10)(11). Both the carbohydrate epitopes and the protein components have been implicated in these roles (7,8,12), although the exact epitopes involved are still unclear. The study of glycosylation in C. albicans will therefore increase our understanding of the host-fungus interaction.…”

mentioning

confidence: 99%

Candida albicans Pmr1p, a Secretory Pathway P-type Ca2+/Mn2+-ATPase, Is Required for Glycosylation and Virulence

Bates

MacCallum

Bertram

et al. 2005

Journal of Biological Chemistry

179

213

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The cell surface of Candida albicans is the immediate point of contact with the host. The outer layer of the cell wall is enriched in highly glycosylated mannoproteins that are implicated in many aspects of the host-fungus interaction. Glycosylation of cell wall proteins is initiated in the endoplasmic reticulum and then elaborated in the Golgi as the protein passes through the secretory pathway. Golgi-bound mannosyltransferases require Mn 2؉ as an essential cofactor. In Saccharomyces cerevisiae, the P-type ATPase Pmr1p transports Ca 2؉ and Mn 2؉ ions into the Golgi. To determine the effect of a gross defect in glycosylation on host-fungus interactions of C. albicans, we disrupted the PMR1 homolog, CaPMR1. This mutation would simultaneously inhibit many Golgi-located, Mn 2؉ -dependent mannosyltransferases. The Capmr1⌬ null mutant was viable in vitro and had no growth defect even on media containing low Ca 2؉ /Mn 2؉ ion concentrations. However, cells grown in these media progressively lost viability upon entering stationary phase. Phosphomannan was almost completely absent, and O-mannan was severely truncated in the null mutant. A defect in N-linked outer chain glycosylation was also apparent, demonstrated by the underglycosylation of surface acid phosphatase. Consistent with the glycosylation defect, the null mutant had a weakened cell wall, exemplified by hypersensitivity to Calcofluor white, Congo red, and hygromycin B and constitutive activation of the cell integrity pathway. In a murine model of systemic infection, the null mutant was severely attenuated in virulence. These results demonstrate the importance of glycosylation for cell wall structure and virulence of C. albicans.

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“…4). Using this (42). Therefore, the ability of both the wild-type and homozygous disruptant C. albicans strains, CAI4 and NGY24 respectively, to adhere to human buccal epithelial cells was tested.…”

mentioning

confidence: 99%

Molecular analysis of CaMnt1p, a mannosyl transferase important for adhesion and virulence of Candida albicans

Buurman

Westwater

Hube

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

129

122

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There is an immediate need for identification of new antifungal targets in opportunistic pathogenic fungi like Candida albicans. In the past, efforts have focused on synthesis of chitin and glucan, which confer mechanical strength and rigidity upon the cell wall. This paper describes the molecular analysis of CaMNT1, a gene involved in synthesis of mannoproteins, the third major class of macromolecule found in the cell wall. CaMNT1 encodes an ␣-1,2-mannosyl transferase, which adds the second mannose residue in a tri-mannose oligosaccharide structure which represents O-linked mannan in C. albicans. The deduced amino acid sequence suggests that CaMnt1p is a type II membrane protein residing in a medial Golgi compartment. The absence of CaMnt1p reduced the ability of C. albicans cells to adhere to each other, to human buccal epithelial cells, and to rat vaginal epithelial cells. Both heterozygous and homozygous Camnt1 null mutants of C. albicans showed strong attenuation of virulence in guinea pig and mouse models of systemic candidosis, which, in guinea pigs, could be attributed to a decreased ability to reach and͞or adhere internal organs. Therefore, correct CaMnt1p-mediated O-linked mannosylation of proteins is critical for adhesion and virulence of C. albicans.

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Molecular bases of adhesion ofCandida albicans

Cited by 107 publications

References 89 publications

Gene expression associated with vegetative incompatibility in Amylostereum areolatum

Gene expression associated with vegetative incompatibility in Amylostereum areolatum

Candida albicans Pmr1p, a Secretory Pathway P-type Ca2+/Mn2+-ATPase, Is Required for Glycosylation and Virulence

Molecular analysis of CaMnt1p, a mannosyl transferase important for adhesion and virulence of Candida albicans

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