Alkaline phosphatase at the cell wall of the yeast phase ofParacoccidioides brasiliensis

Campo-Aasen, I.; Albornoz, María B. de

doi:10.1007/bf01103060

Cited by 5 publications

(5 citation statements)

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“…We reported on a mitochondrial heat-shock chaperone Mdj1 labeled at the P. brasiliensis yeast cell wall (Batista et al, 2006, 2007), which is the preferential site in fully formed mycelia (Dourado et al, unpublished). Alkaline phosphatase activity on the cell wall was demonstrated by histochemical techniques in P. brasiliensis yeast phase (Campo-Aasen and Albornoz, 1994). A secreted 75-kDa protein with phosphatase activity was identified by confocal microscopy and flow cytometry on the cell surface, preferentially at the budding site of P. brasiliensis (Xander et al, 2007).…”

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confidence: 99%

The Paracoccidioides Cell Wall: Past and Present Layers Toward Understanding Interaction with the Host

Puccia¹,

Vallejo²,

Matsuo³

et al. 2011

Front. Microbio.

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The cell wall of pathogenic fungi plays import roles in the interaction with the host, so that its composition and structure may determine the course of infection. Here we present an overview of the current and past knowledge on the cell wall constituents of Paracoccidioides brasiliensis and P. lutzii. These are temperature-dependent dimorphic fungi that cause paracoccidioidomycosis, a systemic granulomatous, and debilitating disease. Focus is given on cell wall carbohydrate and protein contents, their immune-stimulatory features, adhesion properties, drug target characteristics, and morphological phase specificity. We offer a journey toward the future understanding of the dynamic nature of the cell wall and of the changes that may occur when the fungus infects the human host.

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mentioning

confidence: 99%

The Paracoccidioides Cell Wall: Past and Present Layers Toward Understanding Interaction with the Host

Puccia¹,

Vallejo²,

Matsuo³

et al. 2011

Front. Microbio.

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“…Protein phosphatases may exist in soluble [4,12] or secreted forms [13–20], or even remain attached to the outer surface of the inner membrane [21–23] or the cell wall [24,25]. In this context, the ectophosphatases are surface membrane-bound proteins whose active site faces the extracellular medium [26–28].…”

Section: Occurrence Of Ectophosphatase Activities In Fungi Cellsmentioning

confidence: 99%

“…In fungi, ectophosphatases have been described in a large number of species, including Saccharomyces cerevisiae [25], Sporothrix schenckii [32], Paracocciodiodes brasiliensis [24], Candida parapsilosis [33,34], Kluyveromyces marxianus [35], Aspergillus fumigatus [36], Fosencaea pedrosoi [37,38], Cryptococcus neoformans [39], Pseudallescheria boydii [40], Candida albicans [41], Rhinocladiella aquaspersa [42] and Metarhizium anisopliae [43]. It is noteworthy that this review focuses on medically relevant fungal species.…”

Section: Occurrence Of Ectophosphatase Activities In Fungi Cellsmentioning

confidence: 99%

“…For this reason, they are classified as phosphomonoesterases (EC 3.1.3). These phosphatases can be classified according to their cellular location, comprising intracellular enzymes [4,12], secreted enzymes [14,17,18] or surface enzymes that can be associated with the plasma membrane [21–23] or cell wall [24,25]. Other important tools for the classification of phosphatases are the use of inhibitors, divalent cations and different pH ranges [45].…”

Section: Biochemical Properties Of Fungal Ectophosphatasesmentioning

confidence: 99%

“…Despite being classified as intracellular enzymes, alkaline phosphatases have also been reported as ecto-enzymes in P. brasiliensis [24], C. parapsilosis [33] and P. boydii [40]. In a study with C. parapsilosis , 24 isolates showed acid ectophosphatase activities; however, five of them also exhibited alkaline phosphatase activities.…”

Section: Biochemical Properties Of Fungal Ectophosphatasesmentioning

confidence: 99%

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Biochemical Properties and Possible Roles of Ectophosphatase Activities in Fungi

Freitas-Mesquita

Meyer‐Fernandes

2014

IJMS

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Ectophosphatases are surface membrane-bound proteins whose active sites face the extracellular medium. These enzymes have been reported in several microorganisms including a large number of medically relevant fungal species. An effective technique for identifying ectophosphatases is performing phosphatase activity assays using living intact cells. Biochemical characterization of these activities has shown their differential modulation by classical phosphatase inhibitors, divalent metals and pH range. The physiological roles of ectophosphatases are not well established; however, it has been suggested that these enzymes play important roles in nutrition, proliferation, differentiation, adhesion, virulence and infection. Adhesion to host cells is the first step in establishing a fungal infection and ectophosphatases may be one of the first parasite proteins that come into contact with the host cells. Several results indicate that ectophosphatase activities increase the capacity of fungi to adhere to the host cells. In this context, the present review provides an overview of recent discoveries related to the occurrence and possible roles of ectophosphatase activities in fungal cells.

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Ectophosphatase activity in the early-diverging fungus Blastocladiella emersonii: Biochemical characterization and possible role on cell differentiation

Gomes-Vieira

Paes-Vieira

Zamboni

et al. 2018

Fungal Genetics and Biology

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Blastocladiella emersonii is an interesting model for studding the evolution of cell differentiation in eukaryotic cell because of its taxonomic position towards the base of the fungal phylogenetic tree and because it undergoes radical morphological and biochemical changes throughout its life cycle. In this work, we biochemically characterized a high alkaline phosphotyrosine phosphatase activity present on the cell surface (ectophosphatase) of B. emersonii. The ectophosphatase activity was strongly inhibited at acidic pH values as well as by specific phosphatase inhibitors, such as sodium orthovanadate and bpv-PHEN. In addition, the enzyme activity was modulated by the extracellular concentration of inorganic phosphate (P) present in both reaction mixture and culture medium. Phosphotyrosine was hydrolysed at the same extent of its analog, p-NPP, while the hydrolysis of phosphothreonine was 2-fold lower, suggesting that a phosphotyrosine ectophosphatase activity is present on the cell surface of B. emersonii. The ectophosphatase activity was also strongly inhibited by EGTA, indicating the participation of Ca ions on catalysis. The hydrolysis of p-NPP was differentially regulated throughout the B. emersonii life cycle, suggesting that the ectophosphatase activity could be involved in cell differentiation processes. In support of this, the addition of bpv-PHEN or vanadate at the beginning of germination inhibited the differentiation of zoospores to germ cells, compared to control or tartrate-treated cells. On the other hand, if the inhibitors are added 15 or 30 min after initiation of germination the inhibitory effect on zoospore germination decreases significantly, suggesting that the phosphotyrosine ectophosphatase activity is important at the first minutes of germination. The addition of vanadate, molybdate and bpv-PHEN during vegetative growth inhibited the enlargement of the cells compared to control or tartrate-treated cells. Finally, vanadate or bpv-PHEN added during sporulation strongly inhibited zoospore biogenesis, indicating an important role of such ectophosphatases in this differentiation process. Taken together, these data show the existence of a high alkaline ectophosphotyrosine phosphatase activity in B. emersonii that is probably tied to cell differentiation processes of the fungus.

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Alkaline phosphatase at the cell wall of the yeast phase ofParacoccidioides brasiliensis

Cited by 5 publications

References 5 publications

The Paracoccidioides Cell Wall: Past and Present Layers Toward Understanding Interaction with the Host

The Paracoccidioides Cell Wall: Past and Present Layers Toward Understanding Interaction with the Host

Biochemical Properties and Possible Roles of Ectophosphatase Activities in Fungi

Ectophosphatase activity in the early-diverging fungus Blastocladiella emersonii: Biochemical characterization and possible role on cell differentiation

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