Effects of caffeine, cyclic 3?, 5? adenosine monophosphate and cyclic 3?, 5? guanosine monophosphate in the development of the mycelial form of Sporothrix schenckii

Valle, Nuri Rodrı́guez-del; Debs-Elias, N.; Alsina, A.

doi:10.1007/bf00437226

Cited by 12 publications

(4 citation statements)

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“…If this is also true for S. schenckii , addition of arachidonic acid to the medium would be expected to stimulate the yeast cell cycle and this was what we observed. We had previously reported that dibutyryl derivatives of cAMP inhibit the yeast to mycelium transition in S. schenckii [4]. …”

Section: Discussionmentioning

confidence: 99%

“…We have reported that in response to different environmental stimuli, S. schenckii unbudded synchronized yeast cells, either proliferate (yeast cell cycle) or engage in a developmental program that includes proliferation accompanied by morphogenesis (yeast to mycelium transition). Dimorphism in S. schenckii , depends on transmembrane signalling pathways that respond to cell density [2,3], external pH [2,3], cyclic nucleotides [4] and extracellular calcium concentration [5]. …”

Section: Introductionmentioning

confidence: 99%

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Cytosolic phospholipase A2: a member of the signalling pathway of a new G protein α subunit in Sporothrix schenckii

et al. 2009

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BackgroundSporothrix schenckii is a pathogenic dimorphic fungus, the etiological agent of sporotrichosis, a lymphocutaneous disease that can remain localized or can disseminate, involving joints, lungs, and the central nervous system. Pathogenic fungi use signal transduction pathways to rapidly adapt to changing environmental conditions and S. schenckii is no exception. S. schenckii yeast cells, either proliferate (yeast cell cycle) or engage in a developmental program that includes proliferation accompanied by morphogenesis (yeast to mycelium transition) depending on the environmental conditions. The principal intracellular receptors of environmental signals are the heterotrimeric G proteins, suggesting their involvement in fungal dimorphism and pathogenicity. Identifying these G proteins in fungi and their involvement in protein-protein interactions will help determine their role in signal transduction pathways.ResultsIn this work we describe a new G protein α subunit gene in S. schenckii, ssg-2. The cDNA sequence of ssg-2 revealed a predicted open reading frame of 1,065 nucleotides encoding a 355 amino acids protein with a molecular weight of 40.9 kDa. When used as bait in a yeast two-hybrid assay, a cytoplasmic phospholipase A2 catalytic subunit was identified as interacting with SSG-2. The sspla2 gene, revealed an open reading frame of 2538 bp and encoded an 846 amino acid protein with a calculated molecular weight of 92.62 kDa. The principal features that characterize cPLA2 were identified in this enzyme such as a phospholipase catalytic domain and the characteristic invariable arginine and serine residues. A role for SSPLA2 in the control of dimorphism in S. schenckii is suggested by observing the effects of inhibitors of the enzyme on the yeast cell cycle and the yeast to mycelium transition in this fungus. Phospholipase A2 inhibitors such as AACOCF3 (an analogue of archidonic acid) and isotetrandrine (an inhibitor of G protein PLA2 interactions) were found to inhibit budding by yeasts induced to re-enter the yeast cell cycle and to stimulate the yeast to mycelium transition showing that this enzyme is necessary for the yeast cell cycle.ConclusionA new G protein α subunit gene was characterized in S. schenckii and protein-protein interactions studies revealed this G protein alpha subunit interacts with a cPLA2 homologue. The PLA2 homologue reported here is the first phospholipase identified in S. schenckii and the first time a PLA2 homologue is identified as interacting with a G protein α subunit in a pathogenic dimorphic fungus, establishing a relationship between these G proteins and the pathogenic potential of fungi. This cPLA2 homologue is known to play a role in signal transduction and fungal pathogenesis. Using cPLA2 inhibitors, this enzyme was found to affect dimorphism in S. schenckii and was found to be necessary for the development of the yeast or pathogenic form of the fungus.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cytosolic phospholipase A2: a member of the signalling pathway of a new G protein α subunit in Sporothrix schenckii

et al. 2009

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“…Sporothrix is a true dimorphic fungus whose morphology depends on temperature, pH, and other factors, such as cyclic nucleotides [ 13 , 14 ]. At 25–28 °C and an acidic pH, it develops as mycelium, which is considered as the saprophytic phase whereas at higher temperatures (32–37 °C) and a pH of 7.0–7.5, it grows as yeast-like cells, which is the morphotype frequently isolated from infected tissues [ 13 , 14 , 15 ]. Hyphae form either primary or sympodial and secondary or sessile conidia [ 16 , 17 , 18 , 19 , 20 ].…”

Section: Sporothrix and Sporotrichosismentioning

confidence: 99%

“…These species exhibit variations in virulence, transmission, and geographical distribution. Sporothrix is a true dimorphic fungus whose morphology depends on temperature, pH, and other factors, such as cyclic nucleotides [13,14]. At 25-28 °C and an acidic pH, it develops as mycelium, which is considered as the saprophytic phase whereas at higher temperatures (32-37 °C) and a pH of 7.0-7.5, it grows as yeast-like cells, which is the morphotype frequently isolated from infected tissues [13][14][15].…”

Section: General Aspectsmentioning

confidence: 99%

Fungal Glycosidases in Sporothrix Species and Candida albicans

Ortiz-Ramírez,

Cuéllar-Cruz,

Villagómez-Castro

et al. 2023

JoF

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Glycoside hydrolases (GHs) are enzymes that participate in many biological processes of fungi and other organisms by hydrolyzing glycosidic linkages in glycosides. They play fundamental roles in the degradation of carbohydrates and the assembly of glycoproteins and are important subjects of studies in molecular biology and biochemistry. Based on amino acid sequence similarities and 3-dimensional structures in the carbohydrate-active enzyme (CAZy), they have been classified in 171 families. Members of some of these families also exhibit the activity of trans-glycosydase or glycosyl transferase (GT), i.e., they create a new glycosidic bond in a substrate instead of breaking it. Fungal glycosidases are important for virulence by aiding tissue adhesion and colonization, nutrition, immune evasion, biofilm formation, toxin release, and antibiotic resistance. Here, we review fungal glycosidases with a particular emphasis on Sporothrix species and C. albicans, two well-recognized human pathogens. Covered issues include a brief account of Sporothrix, sporotrichosis, the different types of glycosidases, their substrates, and mechanism of action, recent advances in their identification and characterization, their potential biotechnological applications, and the limitations and challenges of their study given the rather poor available information.

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Yeast-Hyphal Dimorphism

Gow

1995

The Growing Fungus

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Effects of caffeine, cyclic 3?, 5? adenosine monophosphate and cyclic 3?, 5? guanosine monophosphate in the development of the mycelial form of Sporothrix schenckii

Cited by 12 publications

References 12 publications

Cytosolic phospholipase A2: a member of the signalling pathway of a new G protein α subunit in Sporothrix schenckii

Cytosolic phospholipase A2: a member of the signalling pathway of a new G protein α subunit in Sporothrix schenckii

Fungal Glycosidases in Sporothrix Species and Candida albicans

Yeast-Hyphal Dimorphism

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