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.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Essen LO,Vogt MS,Mösch HU

doi

10.1515/hsz-2020-0199

subject

Has Abstract

pub_date

2020-11-26 00:00:00

pages

1389-1405

issue

12

eissn

1431-6730

issn

1437-4315

pii

/j/bchm.ahead-of-print/hsz-2020-0199/hsz-2020-0199

journal_volume

401

pub_type

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