グリコカリックスの構造解明(Structure of the glycocalix)

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2025-03-21 マックス・プランク研究所(MPG)

マックス・プランク研究所の研究チームは、緑藻クラミドモナスの鞭毛に存在するグリコカリックスの構造を詳細に解析しました。クライオ電子トモグラフィーにより、鞭毛は外側からFMG1タンパク質層、グリコカリックス、膜、アクソネームの順に構成されていることを確認。特に外側のタンパク質層が細胞の接着機能に関与することが示され、細胞間相互作用や接着機構の理解に新たな知見を提供します。

<関連情報>

毛様体被膜を解きほぐす:毛様体糖鎖の高分解能構造と機能 Unwrapping the Ciliary Coat: High-Resolution Structure and Function of the Ciliary Glycocalyx

Lara M. Hoepfner, Adrian P. Nievergelt, Fabrizio Matrino, Martin Scholz, Helen E. Foster, Jonathan Rodenfels, Alexander von Appen, Michael Hippler, Gaia Pigino
Advanced Science  Published: 05 March 2025
DOI:https://doi.org/10.1002/advs.202413355

グリコカリックスの構造解明(Structure of the glycocalix)

Abstract

The glycocalyx, a highly heterogeneous glycoprotein layer of cilia regulates adhesion and force transduction and is involved in signaling. The high-resolution molecular architecture of this layer is currently not understood. The structure of the ciliary coat is described in the green alga Chlamydomonas reinhardtii by cryo-electron tomography and proteomic approaches and the high-resolution cryoEM structure of the main component, FMG1B is solved. FMG1B is described as a mucin orthologue which lacks the major O-glycosylation of mammalian mucins but is N-glycosylated. FMG1A, a previously undescribed isoform of FMG1B is expressed in C. reinhardtii. By microflow-based adhesion assays, increased surface adhesion in the glycocalyx deficient double-mutant fmg1b-fmg1a is observed. It is found this mutant is capable of surface-gliding, with neither isoform required for extracellular force transduction by intraflagellar transport. The results find FMG1 to form a protective layer with adhesion-regulative instead of adhesion-conferring properties and an example of an undescribed class of mucins.

生物工学一般
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