scholarly journals Glycoprotein Hypersecretion Alters the Cell Wall in Trichoderma reesei Strains Expressing the Saccharomyces cerevisiae Dolichylphosphate Mannose Synthase Gene

2006 ◽  
Vol 72 (12) ◽  
pp. 7778-7784 ◽  
Author(s):  
Urszula Perlińska-Lenart ◽  
Jacek Orłowski ◽  
Agnieszka E. Laudy ◽  
Ewa Zdebska ◽  
Grażyna Palamarczyk ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Trichoderma Reesei ◽  
Morphological Characterization ◽  
Protein Glycosylation ◽  
Fungal Cell Wall ◽  
Ultrastructural Changes ◽  
Calcofluor White ◽  
Fungal Cell ◽  
Gene Coding

ABSTRACT Expression of the Saccharomyces cerevisiae DPM1 gene (coding for dolichylphosphate mannose synthase) in Trichoderma reesei (Hypocrea jecorina) increases the intensity of protein glycosylation and secretion and causes ultrastructural changes in the fungal cell wall. In the present work, we undertook further biochemical and morphological characterization of the DPM1-expressing T. reesei strains. We established that the carbohydrate composition of the fungal cell wall was altered with an increased amount of N-acetylglucosamine, suggesting an increase in chitin content. Calcofluor white staining followed by fluorescence microscopy indicated changes in chitin distribution. Moreover, we also observed a decreased concentration of mannose and alkali-soluble β-(1,6) glucan. A comparison of protein secretion from protoplasts with that from mycelia showed that the cell wall created a barrier for secretion in the DPM1 transformants. We also discuss the relationships between the observed changes in the cell wall, increased protein glycosylation, and the greater secretory capacity of T. reesei strains expressing the yeast DPM1 gene.

scholarly journals Protein Glycosylation inAspergillus fumigatusIs Essential for Cell Wall Synthesis and Serves as a Promising Model of Multicellular Eukaryotic Development

2012 ◽  
Vol 2012 ◽  
pp. 1-21 ◽  
Author(s):  
Cheng Jin
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Posttranslational Modification ◽  
Mammalian Cells ◽  
Protein Glycosylation ◽  
Cell Wall Synthesis ◽  
Fungal Cell ◽  
Multiple Functions ◽  
Significant Attention

Glycosylation is a conserved posttranslational modification that is found in all eukaryotes, which helps generate proteins with multiple functions. Our knowledge of glycosylation mainly comes from the investigation of the yeastSaccharomyces cerevisiaeand mammalian cells. However, during the last decade, glycosylation in the human pathogenic moldAspergillus fumigatushas drawn significant attention. It has been revealed that glycosylation inA. fumigatusis crucial for its growth, cell wall synthesis, and development and that the process is more complicated than that found in the budding yeastS. cerevisiae. The present paper implies that the investigation of glycosylation inA. fumigatusis not only vital for elucidating the mechanism of fungal cell wall synthesis, which will benefit the design of new antifungal therapies, but also helps to understand the role of protein glycosylation in the development of multicellular eukaryotes. This paper describes the advances in functional analysis of protein glycosylation inA. fumigatus.

scholarly journals Deletion of YLR358C Contributes to Reduce Cell Wall Integrity in Saccharomyces Cerevisiae

2022 ◽  
Author(s):  
Yu Zhang ◽  
Mengyan Li ◽  
Hanying Wang ◽  
Juqing Deng ◽  
Jianxing Liu ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Sodium Dodecyl ◽  
Wall Stress ◽  
Pathogenic Fungi ◽  
Cell Wall Integrity ◽  
Calcofluor White ◽  
Fungal Cell ◽  
Reading Frame ◽  
Stress Signals

Abstract The mechanism of fungal cell wall synthesis and assembly is still unclear. Saccharomyces cerevisiae (S. cerevisiae) and pathogenic fungi are conserved in cell wall construction and response to stress signals, and often respond to cell wall stress through activated cell wall integrity (CWI) pathways. Whether the YLR358C open reading frame regulates CWI remains unclear. This study found that the growth of S. cerevisiae with YLR358C knockout was significantly inhibited on the medium containing different concentrations of cell wall interfering agents Calcofluor White (CFW), Congo Red (CR) and sodium dodecyl sulfate (SDS). CFW staining showed that the cell wall chitin was down-regulated, and transmission electron microscopy also observed a decrease in cell wall thickness. Transcriptome sequencing and analysis showed that YLR358C gene may be involved in the regulation of CWI signaling pathway. It was found by qRT-PCR that WSC3, SWI4 and HSP12 were differentially expressed after YLR358C was knocked out. The above results suggest that YLR358C may regulate the integrity of the yeast cell walls and has some potential for application in fermentation.

scholarly journals Saccharomyces cerevisiae HOC1, a Suppressor of pkc1, Encodes a Putative Glycosyltransferase

Genetics ◽  
1997 ◽  
Vol 145 (3) ◽  
pp. 637-645 ◽  
Author(s):  
Aaron M Neiman ◽  
Vijay Mhaiskar ◽  
Vladimir Manus ◽  
Francis Galibert ◽  
Neta Dean
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Cell Lysis ◽  
Integral Membrane Protein ◽  
Protein Glycosylation ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Calcofluor White ◽  
Kinase C

The Saccharomyces cerevisiae gene PKC1 encodes a protein kinase C isozyme that regulates cell wall synthesis. Here we describe the characterization of HOC1, a gene identified by its ability to suppress the cell lysis phenotype of pkc1-371 cells. The HOC1 gene (Homologous to OCH1) is predicted to encode a type II integral membrane protein that strongly resembles Och1p, an α-1,6-mannosyltransferase. Immunofluorescence studies localized Hoc1p to the Golgi apparatus. While overexpression of HOC1 rescued the pkc1-371 temperature-sensitive cell lysis phenotype, disruption of HOC1 lowered the restrictive temperature of the pkc1-371 allele. Disruption of HOC1 also resulted in hypersensitivity to Calcofluor White and hygromycin B, phenotypes characteristic of defects in cell wall integrity and protein glycosylation, respectively. The function of HOC1 appears to be distinct from that of OCH1. Taken together, these results suggest that HOC1 encodes a Golgi-localized putative mannosyltransferase required for the proper construction of the cell wall.

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.

Recent Status and Advancements in the Development of Antifungal Agents: Highlights on Plant and Marine Based Antifungals

2019 ◽  
Vol 19 (10) ◽  
pp. 812-830 ◽  
Author(s):  
P. Marie Arockianathan ◽  
Monika Mishra ◽  
Rituraj Niranjan
Keyword(s):  
Cell Wall ◽  
Antifungal Agents ◽  
Fungal Diseases ◽  
Fungal Cell Wall ◽  
Fungal Resistance ◽  
Ergosterol Biosynthesis ◽  
Fungal Cell ◽  
Ergosterol Synthesis ◽  
Glucan Synthesis ◽  
Anti Fungal

The developing resistance in fungi has become a key challenge, which is being faced nowadays with the available antifungal agents in the market. Further search for novel compounds from different sources has been explored to meet this problem. The current review describes and highlights recent advancement in the antifungal drug aspects from plant and marine based sources. The current available antifungal agents act on specific targets on the fungal cell wall, like ergosterol synthesis, chitin biosynthesis, sphingolipid synthesis, glucan synthesis etc. We discuss some of the important anti-fungal agents like azole, polyene and allylamine classes that inhibit the ergosterol biosynthesis. Echinocandins inhibit β-1, 3 glucan synthesis in the fungal cell wall. The antifungals poloxins and nikkomycins inhibit fungal cell wall component chitin. Apart from these classes of drugs, several combinatorial therapies have been carried out to treat diseases due to fungal resistance. Recently, many antifungal agents derived from plant and marine sources showed potent activity. The renewed interest in plant and marine derived compounds for the fungal diseases created a new way to treat these resistant strains which are evident from the numerous literature publications in the recent years. Moreover, the compounds derived from both plant and marine sources showed promising results against fungal diseases. Altogether, this review article discusses the current antifungal agents and highlights the plant and marine based compounds as a potential promising antifungal agents.

Fungal Cell Wall‐Graphene Oxide Microcomposite Membrane for Organic Solvent Nanofiltration

2021 ◽  
pp. 2100110
Author(s):  
Liyuan Zhang ◽  
Mengchen Zhang ◽  
Gongping Liu ◽  
Wanqin Jin ◽  
Xiaoyan Li
Keyword(s):  
Cell Wall ◽  
Graphene Oxide ◽  
Organic Solvent ◽  
Fungal Cell Wall ◽  
Fungal Cell ◽  
Organic Solvent Nanofiltration
Sign in / Sign up

Export Citation Format

Share Document