Rbt1 protein domains analysis in Candida albicans brings insights into hyphal surface modifications and Rbt1 potential role during adhesion and biofilm formation

PloS One
Céline MonniotMathias L Richard

Abstract

Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces independently of its morphological state, heterologous expression and promoter swap strategies were applied. The N-terminal domain with features typical of the Flo11 superfamily was found to be essential for adhesiveness to polystyrene through an increase in cell surface hydrophobicity. A 42 amino acid-long domain localized in the central part of the protein was shown to enhance the aggregation function. We demonstrated that a VTTGVVVVT motif within the 42 amino acid domain displayed a high β-aggregation potential and was responsible for cell-to-cell interactions by promoting the aggregation of hyphae. Finally, we showed through constitutive expression that while Rbt1 was directly accessible to antibodies in hyphae, it was not so in yeast. Similar results were obtained for another cell wall protein, namely Iff8, and suggested that modification of the cell wall structure between yeas...Continue Reading

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Citations

Dec 24, 2015·Frontiers in Microbiology·Elvira MarínConcha Gil
Jun 6, 2015·Journal of Molecular Recognition : JMR·C FormosaE Dague
Oct 22, 2015·Annual Review of Microbiology·Clarissa J Nobile, Alexander D Johnson
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Jul 18, 2015·Microbiology Spectrum·Jigar V Desai, Aaron P Mitchell
Apr 12, 2020·Mycopathologia·Patrícia Pimentel de BarrosJuliana Campos Junqueira

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Methods Mentioned

BETA
atomic force microscopy
PCR
electrophoresis
fluorescence microscopy
flow cytometry
light microscopy

Software Mentioned

big
Ismatec
PI Fungal Predictor
FlowMax

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