Candida glabrata displays pseudohyphal growth

The ability to undergo morphological change has been reported as an advantageous trait in fungal pathogenesis. Here we demonstrate that Candida glabrata ATCC2001, like diploid Saccharomyces cerevisiae strains, forms elongated chains of pseudohyphal cells on solid nitrogen starvation media (SLAD). Constrictions were apparent between adjoining cells; no parallel-sided hyphae were seen and pseudohyphae invaded the agar. When SLAD was supplemented with ammonium sulfate both C. glabrata and diploid S. cerevisiae strains lost their ability to undergo pseudohyphal growth. However, on this media C. glabrata yeast cells invaded the agar in a similar fashion to the invasive growth mode exhibited by haploid strains of S. cerevisiae cultured on rich media such as YPD. C. glabrata was not capable of invading YPD demonstrating that the process of filamentation is distinct in these two fungi. To our knowledge this is the first report to demonstrate that C. glabrata can undergo morphological change and grow as an invasive filamentous organism

Candida glabratadisplays pseudohyphal growth

Study Break. Food! Coffee! Good Vibes!https://larc.cardozo.yu.edu/flyers-2017-2018/1093/thumbnail.jp

Analysis of isoleucyl-tRNA synthetase genes from Tetrahymena thermophila and Saccharomyces cerevisiae

Isoleucyl-tRNA synthetase genes from the yeast Saccharomyces cerevisiae and the ciliated protozoan Tetrahymena thermophila were sequenced. The intronless S. cerevisiae gene (ILS1) encodes a putative polypeptide of 1072 amino acids. Two putative promoter elements were identified, one for general amino acid control and one for constitutive transcription. A heat shock protein gene lies upstream of ILS1. The T. thermophila isoleucyl-tRNA synthetase gene (ilsA: formerly cupC) has eight introns, four transcription start sites, and codes for a putative polypeptide of 1081 amino acids with two leucine-zippers. These eukaryotic isoleucyl-tRNA synthetases are 47% identical. They are compared to homologous enzymes from Escherichia coli and an archaebacterium, and to other aminoacyl-tRNA synthetases.Intron sequences and junctions from T. thermophila and other eukaryotes were analyzed and all but yeast and mammalian introns were found to be A + T enriched. T. thermophila transcription start sites were analyzed and occur at a T or an A within the consensus sequence (A/T)$sb{ rm n}$ T A A (A)$ sb{ rm n}.

Repression of Hyphal Proteinase Expression by the Mitogen-Activated Protein (MAP) Kinase Phosphatase Cpp1p of Candida albicans Is Independent of the MAP Kinase Cek1p

Cpp1p is a putative mitogen-activated protein (MAP) kinase phosphatase that suppresses Candida albicans hyphal formation at 25°C through its probable substrate, the Cek1p filamentation MAP kinase. Here we report that expression of the serum-induced genes SAP4-6 and HYR1 increased several fold in hyphal forms of a cpp1/cpp1 null mutant, while the rate and extent of hyphal development up to 5 h were normal. Therefore, we provide evidence that Cpp1p represses hyphal gene expression by acting through a Cek1p-independent mechanism. SAP4-6 and HYR1 transcripts were undetectable in a null mutant of another key regulator of filamentation, Efg1p; thus, Efg1p and Cpp1p oppose each other during the expression of these genes in hyphal forms

Derepressed Hyphal Growth and Reduced Virulence in a VH1 Family-related Protein Phosphatase Mutant of the Human Pathogen Candida albicans

Mitogen-activated protein (MAP) kinases are pivotal components of eukaryotic signaling cascades. Phosphorylation of tyrosine and threonine residues activates MAP kinases, but either dual-specificity or monospecificity phosphatases can inactivate them. The Candida albicans CPP1 gene, a structural member of the VH1 family of dual- specificity phosphatases, was previously cloned by its ability to block the pheromone response MAP kinase cascade in Saccharomyces cerevisiae. Cpp1p inactivated mammalian MAP kinases in vitro and acted as a tyrosine-specific enzyme. In C. albicans a MAP kinase cascade can trigger the transition from the budding yeast form to a more invasive filamentous form. Disruption of the CPP1 gene in C. albicans derepressed the yeast to hyphal transition at ambient temperatures, on solid surfaces. A hyphal growth rate defect under physiological conditions in vitro was also observed and could explain a reduction in virulence associated with reduced fungal burden in the kidneys seen in a systemic mouse model. A hyper-hyphal pathway may thus have some detrimental effects on C. albicans cells. Disruption of the MAP kinase homologue CEK1 suppressed the morphological effects of the CPP1 disruption in C. albicans. The results presented here demonstrate the biological importance of a tyrosine phosphatase in cell-fate decisions and virulence in C. albicans

Roles of the Candida albicans Mitogen-Activated Protein Kinase Homolog, Cek1p, in Hyphal Development and Systemic Candidiasis

Extracellular signal-regulated protein kinase (ERK, or mitogen-activated protein kinase [MAPK]) regulatory cascades in fungi turn on transcription factors that control developmental processes, stress responses, and cell wall integrity. CEK1 encodes a Candida albicans MAPK homolog (Cek1p), isolated by its ability to interfere with the Saccharomyces cerevisiae MAPK mating pathway. C. albicans cells with a deletion of the CEK1 gene are defective in shifting from a unicellular budding colonial growth mode to an agar-invasive hyphal growth mode when nutrients become limiting on solid medium with mannitol as a carbon source or on glucose when nitrogen is severely limited. The same phenotype is seen in C. albicans mutants in which the homologs (CST20, HST7, and CPH1) of the S. cerevisiae STE20, STE7, and STE12 genes are disrupted. In S. cerevisiae, the products of these genes function as part of a MAPK cascade required for mating and invasiveness of haploid cells and for pseudohyphal development of diploid cells. Epistasis studies revealed that the C. albicans CST20, HST7, CEK1, and CPH1 gene products lie in an equivalent, canonical, MAPK cascade. While Cek1p acts as part of the MAPK cascade involved in starvation-specific hyphal development, it may also play independent roles in C. albicans. In contrast to disruptions of the HST7 and CPH1 genes, disruption of the CEK1 gene adversely affects the growth of serum-induced mycelial colonies and attenuates virulence in a mouse model for systemic candidiasis