Ectophosphatase activity in Candida albicans influences fungal adhesion: study between HIV-positive and HIV-negative isolates

Portela, MB; Kneipp, LF; Souza, Ivete Pomarico Ribeiro de; Holandino, Carla; Alviano, CS; Meyer-Fernandes, JR; Soares, RM De Araújo

doi:10.1111/j.1601-0825.2009.01644.x

Cited by 21 publications

(17 citation statements)

References 45 publications

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“…Extracellular acid phosphatase activity has been detected in multiple fungal species, including C. neoformans (8, 17, 52). Extracellular APases provide fungal cells with a source of inorganic phosphate, as evidenced by phosphate-dependent expression of these enzymes (11, 16–18).…”

Section: Discussionmentioning

confidence: 99%

“…Phospholipase B1 (Plb1) and laccase are two well-characterized virulence factors that are canonically secreted by C. neoformans but also reside at the membrane and/or cell wall following their transport through the secretory pathway (1–6). Extracellular acid phosphatase (APase) is produced by a large majority of C. neoformans strains (predominantly serotype A) isolated from patients with AIDS (7), by other fungal pathogens, including Candida species (8, 9), Sporothrix schenckii (10), and Aspergillus fumigatus (11), by pathogenic bacteria (12), and by protozoa (13, 14). Acid phosphatases have also been reported to facilitate adhesion of C. neoformans to host cells (15).…”

Section: Introductionmentioning

confidence: 99%

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Identification of Aph1, a Phosphate-Regulated, Secreted, and Vacuolar Acid Phosphatase in Cryptococcus neoformans

Lev

Crossett

Young

et al. 2014

mBio

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Cryptococcus neoformans strains isolated from patients with AIDS secrete acid phosphatase, but the identity and role of the enzyme(s) responsible have not been elucidated. By combining a one-dimensional electrophoresis step with mass spectrometry, a canonically secreted acid phosphatase, CNAG_02944 (Aph1), was identified in the secretome of the highly virulent serotype A strain H99. We created an APH1 deletion mutant (Δaph1) and showed that Δaph1-infected Galleria mellonella and mice survived longer than those infected with the wild type (WT), demonstrating that Aph1 contributes to cryptococcal virulence. Phosphate starvation induced APH1 expression and secretion of catalytically active acid phosphatase in the WT, but not in the Δaph1 mutant, indicating that Aph1 is the major extracellular acid phosphatase in C. neoformans and that it is phosphate repressible. DsRed-tagged Aph1 was transported to the fungal cell periphery and vacuoles via endosome-like structures and was enriched in bud necks. A similar pattern of Aph1 localization was observed in cryptococci cocultured with THP-1 monocytes, suggesting that Aph1 is produced during host infection. In contrast to Aph1, but consistent with our previous biochemical data, green fluorescent protein (GFP)-tagged phospholipase B1 (Plb1) was predominantly localized at the cell periphery, with no evidence of endosome-mediated export. Despite use of different intracellular transport routes by Plb1 and Aph1, secretion of both proteins was compromised in a Δsec14-1 mutant. Secretions from the WT, but not from Δaph1, hydrolyzed a range of physiological substrates, including phosphotyrosine, glucose-1-phosphate, β-glycerol phosphate, AMP, and mannose-6-phosphate, suggesting that the role of Aph1 is to recycle phosphate from macromolecules in cryptococcal vacuoles and to scavenge phosphate from the extracellular environment.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification of Aph1, a Phosphate-Regulated, Secreted, and Vacuolar Acid Phosphatase in Cryptococcus neoformans

Lev

Crossett

Young

et al. 2014

mBio

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“…Several studies have demonstrated that ecto-phosphatase activities are involved in cell adhesion and invasion of distinct microorganisms, including bacteria (Ivanov et al 2005 ), fungal cells (Kneipp et al 2004 ;Collopy-Junior et al 2006 ;Kiffer-Moreira et al 2007 ;Portela et al 2010 ;Kneipp et al 2012 ;CosentinoGomes et al 2013 ) and protozoa Aguirre-García et al 2002 ;Anaya-Ruiz et al 2003 ;Dos Santos et al 2012 ). Protein tyrosine phosphatases are increasingly recognized as important effectors of host-pathogen interactions (Heneberg 2012 ).…”

Section: Ecto-phosphatases As Virulence Markers: Possible Roles In Admentioning

confidence: 98%

Ecto-nucleotidases and Ecto-phosphatases from Leishmania and Trypanosoma Parasites

Freitas-Mesquita

Meyer‐Fernandes

2013

Subcellular Biochemistry

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Ecto-enzymes can be defined as membrane-bound proteins that have their active site facing the extracellular millieu. In trypanosomatids, the physiological roles of these enzymes remain to be completed elucidated; however, many important events have already been related to them, such as the survival of parasites during their complex life cycle and the successful establishment of host infection. This chapter focuses on two remarkable classes of ecto-enzymes: ecto-nucleotidases and ecto-phosphatases, summarizing their occurrence and possible physiological roles in Leishmania and Trypanosoma genera. Ecto-nucleotidases are characterized by their ability to hydrolyze extracellular nucleotides, playing an important role in purinergic signaling. By the action of these ecto-enzymes, parasites are capable of modulating the host immune system, which leads to a successful parasite infection. Furthermore, ecto-nucleotidases are also involved in the purine salvage pathway, acting in the generation of nucleosides that are able to cross plasma membrane via specialized transporters. Another important ecto-enzyme present in a vast number of pathogenic organisms is the ecto-phosphatase. These enzymes are able to hydrolyze extracellular phosphorylated substrates, releasing free inorganic phosphate that can be internalized by the cell, crossing the plasma membrane through a Pi-transporter. Ecto-phosphatases are also involved in the invasion and survival of parasite in the host cells. Several alternative functions have been suggested for these enzymes in parasites, such as participation in their proliferation, differentiation, nutrition and protection. In this context, the present chapter provides an overview of recent discoveries related to the occurrence of ecto-nucleotidase and ecto-phosphatase activities in Leishmania and Trypanosoma parasites.

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“…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%

“…The p -NPP hydrolysis generates inorganic phosphate (P i ) and p -nitrophenol ( p -NP), which turns yellow under alkaline conditions and can be quantified spectrophotometrically. This approach was performed with S. cerevisiae [25], C. parapsilosis [33,34], F. pedrosoi [37,38], C. neoformans [39], P. boydii [40], C. albicans [41], R. aquaspersa [42] and M. anisopliae [43]. …”

Section: Occurrence Of Ectophosphatase Activities In Fungi Cellsmentioning

confidence: 99%

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 Candida albicans influences fungal adhesion: study between HIV-positive and HIV-negative isolates

Cited by 21 publications

References 45 publications

Identification of Aph1, a Phosphate-Regulated, Secreted, and Vacuolar Acid Phosphatase in Cryptococcus neoformans

Identification of Aph1, a Phosphate-Regulated, Secreted, and Vacuolar Acid Phosphatase in Cryptococcus neoformans

Ecto-nucleotidases and Ecto-phosphatases from Leishmania and Trypanosoma Parasites

Biochemical Properties and Possible Roles of Ectophosphatase Activities in Fungi

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