The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae is an adhesin without mannose-binding activity

Goossens, Katty; Willaert, Ronnie

doi:10.1111/j.1567-1364.2011.00766.x

Cited by 30 publications

(32 citation statements)

References 58 publications

(154 reference statements)

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“…Interestingly, the NetOGlyc tool predicts no N-glycosylation site in the ScFlo11A domain, but identifies at least S36 in the neck subdomain as a putative O-glycosylation site ( Figure S4). Indeed, O-glycosylation and a lack of N-glycosylation were recently shown for recombinant ScFlo11A domains, which were overproduced in the yeast Pichia pastoris (Goossens and Willaert, 2012).…”

Section: Resultsmentioning

confidence: 98%

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Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands

et al. 2015

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Saccharomyces cerevisiae harbors a family of GPI-anchored cell wall proteins for interaction with its environment. The flocculin Flo11, a major representative of these fungal adhesins, confers formation of different types of multicellular structures such as biofilms, flors, or filaments. To understand these environment-dependent growth phenotypes on a molecular level, we solved the crystal structure of the N-terminal Flo11A domain at 0.89-Å resolution. Besides a hydrophobic apical region, the Flo11A domain consists of a β sandwich of the fibronectin type III domain (FN3). We further show that homophilic Flo11-Flo11 interactions and heterophilic Flo11-plastic interactions solely depend on the Flo11A domain and are strongly pH dependent. These functions of Flo11A involve an apical region with its surface-exposed aromatic band, which is accompanied by acidic stretches. Together with electron microscopic reconstructions of yeast cell-cell contact sites, our data suggest that Flo11 acts as a spacer-like, pH-sensitive adhesin that resembles a membrane-tethered hydrophobin.

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Section: Resultsmentioning

confidence: 98%

“…Homophilic ScFlo11A-ScFlo11A Interactions, pH Sensitivity, and Aromatic Bands It was previously suggested that ScFlo11A domains may associate via homophilic interactions (Goossens and Willaert, 2012). To test this hypothesis, we performed SPR analysis with the ScFlo11A-His 6 domain.…”

Section: The Core Of Scflo11a Is a Fibronectin Type III Domainmentioning

confidence: 98%

Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands

et al. 2015

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“…The population at the start, and after seven and fifteen days were compared ( Figure 5). The CMBSVM22 strain possesses the FLO11 gene required for invasive growth [32,[47][48][49], which could clearly be seen on the bottom of the plates. The morphology of the colonies differed after 14 days, the same time when the snowflake flocs were observed.…”

Section: Adaptive Evolution During Continuous Operationmentioning

confidence: 99%

Gravity-Driven Adaptive Evolution of an Industrial Brewer’s Yeast Strain towards a Snowflake Phenotype in a 3D-Printed Mini Tower Fermentor

Conjaerts

Willaert

2017

Fermentation

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Abstract:We designed a mini tower fermentor that is suitable to perform adaptive laboratory evolution (ALE) with gravity imposed as selective pressure, and suitable to evolve a weak flocculating industrial brewers' strain towards a strain with a more extended aggregation phenotype. This phenotype is of particular interest in the brewing industry, since it simplifies yeast removal at the end of the fermentation, and many industrial strains are still not sufficiently flocculent. The flow of particles (yeast cells and flocs) was simulated, and the theoretical retainment advantage of aggregating cells over single cells in the tower fermentor was demonstrated. A desktop stereolithography (SLA) printer was used to construct the mini reactor from transparent methacrylic acid esters resin. The printed structures were biocompatible for yeast growth, and could be sterilised by autoclaving. The flexibility of 3D printing allowed the design to be optimized quickly. During the ALE experiment, yeast flocs were observed within two weeks after the start of the continuous cultivation. The flocs showed a "snowflake" morphology, and were not the result of flocculin interactions, but probably the result of (a) mutation(s) in gene(s) that are involved in the mother/daughter separation process.

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“…Flo11p/Muc1p is a mucin-like protein that belongs to the family of flocculins and is involved in cell-substrate and cell-cell adhesion, invasive growth on agar, and biofilm formation on plastic and liquid surfaces (1,5,(7)(8)(9)(10). It is a CW glycoprotein with a C-terminal glycosylphosphatidylinositol (GPI) anchor, a large and highly O-glycosylated central domain rich in serine and threonine, and a N-terminal domain that mediates homotypic adhesion between cells (7,11). flo11 mutants of flor yeasts cannot form biofilms, demonstrating the role of Flo11p in biofilm formation on liquid surfaces (4,5,(12)(13)(14)(15).…”

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confidence: 99%

FLO11 Gene Is Involved in the Interaction of Flor Strains of Saccharomyces cerevisiae with a Biofilm-Promoting Synthetic Hexapeptide

Zeidan

Carmona

Zara

et al. 2013

Appl Environ Microbiol

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bSaccharomyces cerevisiae "flor" yeasts have the ability to form a buoyant biofilm at the air-liquid interface of wine. The formation of biofilm, also called velum, depends on FLO11 gene length and expression. FLO11 encodes a cell wall mucin-like glycoprotein with a highly O-glycosylated central domain and an N-terminal domain that mediates homotypic adhesion between cells. In the present study, we tested previously known antimicrobial peptides with different mechanisms of antimicrobial action for their effect on the viability and ability to form biofilm of S. cerevisiae flor strains. We found that PAF26, a synthetic tryptophanrich cationic hexapeptide that belongs to the class of antimicrobial peptides with cell-penetrating properties, but not other antimicrobial peptides, enhanced biofilm formation without affecting cell viability in ethanol-rich medium. The PAF26 biofilm enhancement required a functional FLO11 but was not accompanied by increased FLO11 expression. Moreover, fluorescence microscopy and flow cytometry analyses showed that the PAF26 peptide binds flor yeast cells and that a flo11 gene knockout mutant lost the ability to bind PAF26 but not P113, a different cell-penetrating antifungal peptide, demonstrating that the FLO11 gene is selectively involved in the interaction of PAF26 with cells. Taken together, our data suggest that the cationic and hydrophobic PAF26 hexapeptide interacts with the hydrophobic and negatively charged cell wall, favoring Flo11p-mediated cell-tocell adhesion and thus increasing biofilm biomass formation. The results are consistent with previous data that point to glycosylated mucin-like proteins at the fungal cell wall as potential interacting partners for antifungal peptides.

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The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae is an adhesin without mannose-binding activity

Cited by 30 publications

References 58 publications

Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands

Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands

Gravity-Driven Adaptive Evolution of an Industrial Brewer’s Yeast Strain towards a Snowflake Phenotype in a 3D-Printed Mini Tower Fermentor

FLO11 Gene Is Involved in the Interaction of Flor Strains of Saccharomyces cerevisiae with a Biofilm-Promoting Synthetic Hexapeptide

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