scholarly journals Role of Protein Glycosylation in Candida parapsilosis Cell Wall Integrity and Host Interaction

2016 ◽  
Vol 7 ◽  
Author(s):  
Luis A. Pérez-García ◽  
Katalin Csonka ◽  
Arturo Flores-Carreón ◽  
Eine Estrada-Mata ◽  
Erika Mellado-Mojica ◽  
...  
Keyword(s):  
Cell Wall ◽  
Candida Parapsilosis ◽  
Protein Glycosylation ◽  
Cell Wall Integrity ◽  
Host Interaction

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 Role of CpALS4790 and CpALS0660 in Candida parapsilosis Virulence: Evidence from a Murine Model of Vaginal Candidiasis

2020 ◽  
Vol 6 (2) ◽  
pp. 86
Author(s):  
Marina Zoppo ◽  
Fabrizio Fiorentini ◽  
Cosmeri Rizzato ◽  
Mariagrazia Di Luca ◽  
Antonella Lupetti ◽  
...  
Keyword(s):  
Cell Wall ◽  
Murine Model ◽  
Type Strain ◽  
Wild Type Strain ◽  
Candida Parapsilosis ◽  
Vaginal Candidiasis ◽  
Phenotypic Characterization ◽  
Wild Type ◽  
Mutant Strains

The Candida parapsilosis genome encodes for five agglutinin-like sequence (Als) cell-wall glycoproteins involved in adhesion to biotic and abiotic surfaces. The work presented here is aimed at analyzing the role of the two still uncharacterized ALS genes in C. parapsilosis, CpALS4790 and CpALS0660, by the generation and characterization of CpALS4790 and CpALS066 single mutant strains. Phenotypic characterization showed that both mutant strains behaved as the parental wild type strain regarding growth rate in liquid/solid media supplemented with cell-wall perturbing agents, and in the ability to produce pseudohyphae. Interestingly, the ability of the CpALS0660 null mutant to adhere to human buccal epithelial cells (HBECs) was not altered when compared with the wild-type strain, whereas deletion of CpALS4790 led to a significant loss of the adhesion capability. RT-qPCR analysis performed on the mutant strains in co-incubation with HBECs did not highlight significant changes in the expression levels of others ALS genes. In vivo experiments in a murine model of vaginal candidiasis indicated a significant reduction in CFUs recovered from BALB/C mice infected with each mutant strain in comparison to those infected with the wild type strain, confirming the involvement of CpAls4790 and CpAls5600 proteins in C. parapsilosis vaginal candidiasis in mice.

scholarly journals To preserve or to destroy, that is the question: the role of the cell wall integrity pathway in pollen tube growth

2019 ◽  
Vol 52 ◽  
pp. 131-139 ◽  
Author(s):  
Hannes Vogler ◽  
Gorka Santos-Fernandez ◽  
Martin A Mecchia ◽  
Ueli Grossniklaus
Keyword(s):  
Cell Wall ◽  
Pollen Tube ◽  
Pollen Tube Growth ◽  
Cell Wall Integrity ◽  
Tube Growth ◽  
Cell Wall Integrity Pathway

scholarly journals An emerging role of pectic rhamnogalacturonanII for cell wall integrity

2012 ◽  
Vol 7 (2) ◽  
pp. 298-299 ◽  
Author(s):  
Rebecca Reboul ◽  
Raimund Tenhaken
Keyword(s):  
Cell Wall ◽  
Cell Wall Integrity

scholarly journals SUN-Family Protein UvSUN1 Regulates the Development and Virulence of Ustilaginoidea virens

2021 ◽  
Vol 12 ◽  
Author(s):  
Mina Yu ◽  
Junjie Yu ◽  
Huijuan Cao ◽  
Tianqiao Song ◽  
Xiayan Pan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Hyphal Growth ◽  
Cell Wall Integrity ◽  
Signal Recognition ◽  
Phenotypic Analysis ◽  
Ustilaginoidea Virens ◽  
Group I ◽  
Family Protein ◽  
False Smut

Ustilaginoidea virens, the causal agent of rice false smut disease, is an important plant pathogen that causes severe quantitative and qualitative losses in rice worldwide. UvSUN1 is the only member of Group-I SUN family proteins in U. virens. In this work, the role of UvSUN1 in different aspects of the U. virens biology was studied by phenotypic analysis of Uvsun1 knockout strains. We identified that UvSUN1 was expressed during both conidial germination and the infection of rice. Disruption of the Uvsun1 gene affected the hyphal growth, conidiation, morphology of hyphae and conidia, adhesion and virulence. We also found that UvSUN1 is involved in the production of toxic compounds, which are able to inhibit elongation of the germinated seeds. Moreover, RNA-seq data showed that knockout of Uvsun1 resulted in misregulation of a subset of genes involved in signal recognition and transduction system, glycometabolism, cell wall integrity, and secondary metabolism. Collectively, this study reveals that Uvsun1 is required for growth, cell wall integrity and pathogenicity of U. virens, thereby providing new insights into the function of SUN family proteins in the growth and pathogenesis of this pathogen.

scholarly journals Defects in Protein Glycosylation Cause SHO1-Dependent Activation of a STE12 Signaling Pathway in Yeast

Genetics ◽  
2000 ◽  
Vol 155 (3) ◽  
pp. 1005-1018 ◽  
Author(s):  
Paul J Cullen ◽  
Janet Schultz ◽  
Joe Horecka ◽  
Brian J Stevenson ◽  
Yoshifumi Jigami ◽  
...  
Keyword(s):  
Cell Wall ◽  
Genetic Selection ◽  
Protein Glycosylation ◽  
Cell Wall Integrity ◽  
Growth Defect ◽  
Loss Of Function ◽  
Pheromone Response ◽  
Pheromone Response Pathway ◽  
Pathway Activation ◽  
Synthetic Growth

Abstract In haploid Saccharomyces cerevisiae, mating occurs by activation of the pheromone response pathway. A genetic selection for mutants that activate this pathway uncovered a class of mutants defective in cell wall integrity. Partial loss-of-function alleles of PGI1, PMI40, PSA1, DPM1, ALG1, MNN10, SPT14, and OCH1, genes required for mannose utilization and protein glycosylation, activated a pheromone-response-pathway-dependent reporter (FUS1) in cells lacking a basal signal (ste4). Pathway activation was suppressed by the addition of mannose to hexose isomerase mutants pgi1-101 and pmi40-101, which bypassed the requirement for mannose biosynthesis in these mutants. Pathway activation was also suppressed in dpm1-101 mutants by plasmids that contained RER2 or PSA1, which produce the substrates for Dpm1. Activation of FUS1 transcription in the mannose utilization/protein glycosylation mutants required some but not all proteins from three different signaling pathways: the pheromone response, invasive growth, and HOG pathways. We specifically suggest that a Sho1 → Ste20/Ste50 → Ste11 → Ste7 → Kss1 → Ste12 pathway is responsible for activation of FUS1 transcription in these mutants. Because loss of pheromone response pathway components leads to a synthetic growth defect in mannose utilization/protein glycosylation mutants, we suggest that the Sho1 → Ste12 pathway contributes to maintenance of cell wall integrity in vegetative cells.

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