Diversity of GPI-anchored fungal adhesins
Abstract: Selective adhesion of fungal cells to one another and to foreign surfaces is fundamental for the development of multicellular growth forms and the successful colonization of substrates and host organisms. Accordingly, fungi possess diverse cell wall-associated adhesins, mostly large glycoproteins, which present N-terminal adhesion domains at the cell surface for ligand recognition and binding. In order to function as robust adhesins, these glycoproteins must be covalently linkedto the cell wall via C-terminal glycosylphosphatidylinositol (GPI) anchors by transglycosylation. In this review, we summarize the current knowledge on the structural and functional diversity of so far characterized protein families of adhesion domains and set it into a broad context by an in-depth bioinformatics analysis using sequence similarity networks. In addition, we discuss possible mechanisms for the membrane-to-cell wall transfer of fungal adhesins by membrane-anchored Dfg5 transglycosidases.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Diversity of GPI-anchored fungal adhesins ; volume:401 ; number:12 ; year:2020 ; pages:1389-1405 ; extent:017
Biological chemistry ; 401, Heft 12 (2020), 1389-1405 (gesamt 017)
- Creator
- DOI
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10.1515/hsz-2020-0199
- URN
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urn:nbn:de:101:1-2408061723570.176396757953
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 11:02 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Essen, Lars Oliver
- Vogt, Marian Samuel
- Mösch, Hans-Ulrich
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