Glycosylation of Yeast and Fungal Cell Wall Components

1979 ◽  
Vol 7 (2) ◽  
pp. 331-333 ◽  
Author(s):  
PIETER BOER
Keyword(s):  
Cell Wall ◽  
Fungal Cell Wall ◽  
Fungal Cell ◽  
Cell Wall Components ◽  
Wall Components

scholarly journals Exploiting fungal cell wall components in vaccines

2014 ◽  
Vol 37 (2) ◽  
pp. 199-207 ◽  
Author(s):  
Stuart M. Levitz ◽  
Haibin Huang ◽  
Gary R. Ostroff ◽  
Charles A. Specht
Keyword(s):  
Cell Wall ◽  
Fungal Cell Wall ◽  
Fungal Cell ◽  
Cell Wall Components ◽  
Wall Components

scholarly journals Fungal Cell Wall Components Modulate our Immune System

2021 ◽  
pp. 100067
Author(s):  
Benoit Briard ◽  
Thierry Fontaine ◽  
Thirumala-Devi Kanneganti ◽  
Neil A.R. Gow ◽  
Nicolas Papon
Keyword(s):  
Cell Wall ◽  
Immune System ◽  
Fungal Cell Wall ◽  
Fungal Cell ◽  
Cell Wall Components ◽  
Wall Components

scholarly journals The Dual Activity Responsible for the Elongation and Branching of β-(1,3)-Glucan in the Fungal Cell Wall

mBio ◽  
2017 ◽  
Vol 8 (3) ◽  
Author(s):  
Vishukumar Aimanianda ◽  
Catherine Simenel ◽  
Cecile Garnaud ◽  
Cecile Clavaud ◽  
Rui Tada ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Aspergillus Fumigatus ◽  
Fungal Cell Wall ◽  
Carbohydrate Binding ◽  
Fungal Cell ◽  
Cell Wall Components ◽  
Cell Wall Assembly ◽  
Subsequent Event ◽  
Wall Components

ABSTRACTβ-(1,3)-Glucan, the major fungal cell wall component, ramifies through β-(1,6)-glycosidic linkages, which facilitates its binding with other cell wall components contributing to proper cell wall assembly. UsingSaccharomyces cerevisiaeas a model, we developed a protocol to quantify β-(1,6)-branching on β-(1,3)-glucan. PermeabilizedS. cerevisiaeand radiolabeled substrate UDP-(14C)glucose allowed us to determine branching kinetics. A screening aimed at identifying deletion mutants with reduced branching among them revealed only two, thebgl2Δ andgas1Δ mutants, showing 15% and 70% reductions in the branching, respectively, compared to the wild-type strain. Interestingly, a recombinant Gas1p introduced β-(1,6)-branching on the β-(1,3)-oligomers following its β-(1,3)-elongase activity. Sequential elongation and branching activity of Gas1p occurred on linear β-(1,3)-oligomers as well as Bgl2p-catalyzed products [short β-(1,3)-oligomers linked by a linear β-(1,6)-linkage]. The doubleS. cerevisiae gas1Δbgl2Δ mutant showed a drastically sick phenotype. AnScGas1p ortholog, Gel4p fromAspergillus fumigatus, also showed dual β-(1,3)-glucan elongating and branching activity. BothScGas1p andA. fumigatusGel4p sequences are endowed with a carbohydrate binding module (CBM), CBM43, which was required for the dual β-(1,3)-glucan elongating and branching activity. Our report unravels the β-(1,3)-glucan branching mechanism, a phenomenon occurring during construction of the cell wall which is essential for fungal life.IMPORTANCEThe fungal cell wall is essential for growth, morphogenesis, protection, and survival. In spite of being essential, cell wall biogenesis, especially the core β-(1,3)-glucan ramification, is poorly understood; the ramified β-(1,3)-glucan interconnects other cell wall components. Once linear β-(1,3)-glucan is synthesized by plasma membrane-bound glucan synthase, the subsequent event is its branching event in the cell wall space. UsingSaccharomyces cerevisiaeas a model, we identified GH72 and GH17 family glycosyltransferases, Gas1p and Bgl2p, respectively, involved in the β-(1,3)-glucan branching. The sick phenotype of the doubleScgas1Δbgl2Δ mutant suggested that β-(1,3)-glucan branching is essential. In addition toScGas1p, GH72 familyScGas2p andAspergillus fumigatusGel4p, having CBM43 in their sequences, showed dual β-(1,3)-glucan elongating and branching activity. Our report identifies the fungal cell wall β-(1,3)-glucan branching mechanism. The essentiality of β-(1,3)-glucan branching suggests that enzymes involved in the glucan branching could be exploited as antifungal targets.

Sign in / Sign up

Export Citation Format

Share Document