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Diversity of GPI-anchored fungal adhesins

Authors
  • Essen, Lars-Oliver1, 2
  • Vogt, Marian Samuel1
  • Mösch, Hans-Ulrich3, 2
  • 1 Philipps-Universität Marburg, Hans-Meerwein-Straße 4 , (Germany)
  • 2 Philipps-Universität Marburg, Karl-von-Frisch-Str. 6 , (Germany)
  • 3 Philipps-Universität Marburg, Karl-von-Frisch-Str. 8 , (Germany)
Type
Published Article
Journal
Biological Chemistry
Publisher
Walter de Gruyter GmbH
Publication Date
Oct 09, 2020
Volume
401
Issue
12
Pages
1389–1405
Identifiers
DOI: 10.1515/hsz-2020-0199
Source
De Gruyter
Keywords
License
Green

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.

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