
β-1,6-グルカンは、カンジダ・アルビカンスの二層性細胞壁構造の維持、細胞壁の完全性、および菌糸形成に不可欠である。


coremsg

The cell wall of human fungal pathogens plays critical roles as an architectural scaffold and as a target and modulator of the host immune response. Although the cell wall of the pathogenic yeast Candida albicans is intensively studied, one of the major fibrillar components in its cell wall, β-1,6-glucan, has been largely neglected. Here, we show that β-1,6-glucan is essential for bilayered cell wall organization, cell wall integrity and filamentous growth. For the first time, we show that β-1,6-glucan production compensates the defect in mannan elongation in the outer layer of the cell wall. In addition, β-1,6-glucan dynamics are also coordinated by host environmental stimuli and stresses with wall remodeling, where the regulation of β-1,6-glucan structure and chain length is a crucial process. As we point out that β-1,6-glucan is exposed at the yeast surface and modulate immune response, β-1,6-glucan must be considered a key factor in host-pathogen interactions.

### Competing Interest Statement

The authors have declared no competing interest.

β-1,6-glucan plays a central role in the structure and remodeling of the bilaminate fungal cell wall

カンジダ-アルビカンスの二層性細胞壁構造と再構築における-β-1-6-グルカンの中心的役割


カンジダ・アルビカンスの二層性細胞壁構造と再構築における β-1,6-グルカンの中心的役割


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ペクチンの脱メチル化状態がRALF1ペプチドの受容に必要不可欠である


The extracellular matrix plays an integrative role in cellular responses in plants, but its contribution to the signalling of extracellular ligands largely remains to be explored. RAPID ALKALINIZATION FACTORs (RALFs) are extracellular peptide hormones that play pivotal roles in various physiological processes. Here, we address a crucial connection between the demethylation machinery of the cell wall component pectin and RALF1 activity. Pectin is a polysaccharide, contributing to the structural integrity of the cell wall. Our data illustrate that the pharmacological and genetic interference with PECTIN METHYL ESTERASEs (PMEs) abolishes RALF1-induced root growth repression. Our data suggest that positively charged RALF1 peptides bind negatively charged, demethylated pectin with high avidity. We illustrate that the RALF1 association with demethylated pectin is required for its FERONIA-dependent perception, contributing to the control of the extracellular matrix and the regulation of plasma membrane dynamics. Notably, this mode of action is independent of the FER-dependent extracellular matrix sensing mechanism provided by FER interaction with the Leucine-Rich Repeat Extensin (LRX) proteins. We propose that the methylation status of pectin acts as a conceptualizing signalling scaffold for RALF peptides, linking extracellular matrix dynamics to peptide hormone-mediated responses.

### Competing Interest Statement

The authors have declared no competing interest.

Pectin methylesterase activity is required for RALF1 peptide signalling output

ペクチンメチルエステラーゼ活性はralf1ペプチド伝達シグナルの出力に必要である


ペクチンメチルエステラーゼ活性はRALF1ペプチド伝達シグナルの出力に必要である
