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Mycelial forms of Pseudallescheria boydii present ectophosphatase activities

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Abstract

Phosphatase activities were characterized in intact mycelial forms of Pseudallescheria boydii, which are able to hydrolyze the artificial substrate p-nitrophenylphosphate (p-NPP) to p-nitrophenol (p-NP) at a rate of 41.41 ± 2.33 nmol p-NP per h per mg dry weight, linearly with increasing time and with increasing cell density. MgCl2, MnCl2 and ZnCl2 were able to increase the (p-NPP) hydrolysis while CdCl2 and CuCl2 inhibited it. The (p-NPP) hydrolysis was enhanced by increasing pH values (2.5-8.5) over an approximately 5-fold range. High sensitivity to specific inhibitors of alkaline and acid phosphatases suggests the presence of both acid and alkaline phosphatase activities on P. boydii mycelia surface. Cytochemical localization of the acid and alkaline phosphatase showed electron-dense cerium phosphate deposits on the cell wall, as visualized by electron microscopy. The product of p-NPP hydrolysis, inorganic phosphate (Pi), and different inhibitors for phosphatase activities inhibited p-NPP hydrolysis in a dose-dependent manner, but only the inhibition promoted by sodium orthovanadate and ammonium molybdate is irreversible. Intact mycelial forms of P. boydii are also able to hydrolyze phosphoaminoacids with different specificity.

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References

  • Almeida-Amaral EE, Belmont-Firpo R, Vannier-Santos MA, Meyer-Fernandes JR (2006) Leishmania amazonensis: characterization of an ecto-phosphatase activity. Exp Parasitol 114:334–340

    Article  PubMed  CAS  Google Scholar 

  • Arnold WN, Mann LC, Sakai KH, Garrison RG, Coleman PD (1986) The acid phosphatases of Sporothrix schenckii. J Gen Microbiol 132:3421–3432

    PubMed  CAS  Google Scholar 

  • Arnold WN, Sakai KH, Mann LC (1987) Selective inactivation of an extra-cytoplasmic acid phosphatase of Sporothrix schenckii by sodium floride. J Gen Microbiol 133:1503–1509

    PubMed  CAS  Google Scholar 

  • Bakalara N, Santarelli X, Davis C, Baltz T (2000) Purification, cloning and characterization of an acid ectoprotein phosphatase differentially expressed in the infectious bloodstream form of Trypanosoma brucei. J Biol Chem 275:8863–8871

    Article  PubMed  CAS  Google Scholar 

  • Bakerspiegel A (1971) Fungi isolated from keratomycosis in Ontario, Canada. I. Monosporium apiospermum (Allescheria boydii). Sabouraudia 9:109–112

    PubMed  CAS  Google Scholar 

  • Barret WC, DeGnore JP, Konig S, Keng Y-F, Zhang Z-Y, Yim MB, Check PB (1999) Regulation of PTP1B via glutathionylation on the active site cysteine 215. Biochemistry 38:6599–6705

    Article  Google Scholar 

  • Baxter M, Murray IG, Taylor JJ (1996) A case of mycetoma with serological diagnosis of Allescheria boydii. Sabouraudia 5:109–112

    Google Scholar 

  • Belanger PH, Johnston DA, Fratti RA, Zhang M, Filler SG (2002) Endocytosis of Candida albicans by vascular endothelial cells is associated with tyrosine phosphorylation of specific host cells proteins. Cell Microbiol 4:805–812

    Article  PubMed  CAS  Google Scholar 

  • Berenguer J, Diaz-Mediavilla J, Urra D, Muñoz P (1989) Central nervous system infection caused by P. boydii: case report and review. Rev Infect Dis 11:890–896

    PubMed  CAS  Google Scholar 

  • Bliska JB, Galán JE, Falkon S (1993) Signal transduction in the mammalian cell during bacterial attachment and entry. Cell 73:903–920

    Article  PubMed  CAS  Google Scholar 

  • Bliska JB, Guan K, Dixon JE, Falkon S (1991) Tyrosine phosphatase hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc Natl Acad Sci USA 88:1187–1191

    Article  PubMed  CAS  Google Scholar 

  • Bouchara JP, Tronchin G, Chabase D (1995) The search for virulence determinants in Aspergillus fumigatus. Trends Microbiol 3:327–330

    Article  PubMed  CAS  Google Scholar 

  • Braibant M, Content J (2001) The cell surface associated phosphatase activity of Mycobacterium bovis BCG is not regulated by enviromental inorganic phosphate. FEMS Microbiol Lett 195:121–126

    Article  PubMed  CAS  Google Scholar 

  • Bullock WE, Wright SD (1987) Role of adherence-promoting receptors, CR3, LFA-1 and p150, 95, in binding Histoplasma capsulatum in human macrophages. J Exp Med 1:195–210

    Article  Google Scholar 

  • Calderone R, Diamond R, Senté JM, Warmington J, Filler S, Edwards JE (1994) Host cell-fungal interactions. J Med Vet Mycol 32:151–168

    Article  PubMed  Google Scholar 

  • Cohen PTW (1989) The structure and regulation of protein phosphatases. Annu Rev Biochem 58:453–508

    Article  PubMed  CAS  Google Scholar 

  • Collopy-Junior I, Kneipp LF, da Silva FC, Rodrigues ML, Alviano CS, Meyer-Fernandes JR (2006a) Characterization of an ecto-ATPase activity in Fonsecaea pedrosoi. Arch Microbiol 185:355–362

    Article  CAS  Google Scholar 

  • Collopy-Junior I, Esteves FF, Nimrichter L, Rodrigues ML, Alviano CS, Meyer-Fernandes JR (2006b) An ectophosphatase activity in Cryptococcus neoformans. FEMS Yeast Res 6:1010–1017

    Article  CAS  Google Scholar 

  • Denu JM, Tanner KG (2002) Redox regulation of protein phosphatases by hidrogen peroxide: detecting sulfenic acid intermediates and examining reversible inactivation. Methods Enzymol 348:297–305

    Article  PubMed  CAS  Google Scholar 

  • Dickmann MB, Yarden O (2000) Serine/Threonine protein kinases and phosphatases in filamentous fungi. Fungal Genet Biol 26:99–117

    Article  Google Scholar 

  • Dutra PML, Dias FA, Santos MAA, Rodrigues CO, Romeiro A, Attias M, De Souza W, Lopes AHCS, Meyer-Fernandes JR (2001) Secreted phosphatase activities in trypanossomatid parasites of plants modulated by patelet-activating factor. Phytopathology 91:408–414

    Article  CAS  PubMed  Google Scholar 

  • Fernandes EC, Granjeiro JM, Aoyama H, Fonseca V, Meyer-Fernandes JR, Vercesi AE (2003) A metallo phosphatase activity present on the surface of Trypanossoma brucei procyclic forms. Vet Parasitol 118:19–28

    Article  PubMed  CAS  Google Scholar 

  • Fernanado PHP, Panagoda GJ, Samaranayare LP (1999) The relation between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human epithelial cell. APMIS 107:1034–1042

    Article  PubMed  CAS  Google Scholar 

  • Fernandes EC, Meyer-Fernandes JR, Silva-Neto MAC, Vercesi AE (1997) Trypanosoma brucei: ecto-phosphatase activity on the surface of intact procclic forms. Z Naturforsch 52c:351–358

    Google Scholar 

  • Furuya T, Zhong L, Meyer-Fernandes JR, Lu H-G, Moreno SNJ, Docampo R (1998) Ecto-protein tyrosine phosphatase activity in Trypanossoma cruzi infective forms. Mol Biochem Parasitol Today 14:277–281

    Google Scholar 

  • Ginter G, Petutschnig B, Pierer G, Soyer HP, Reischle S, Kern T, de Hoog S (1999) Case report. Atypical cutaneous pesudallescheriosis refractory to antifungal agents. Mycosis 42:507–511

    Article  CAS  Google Scholar 

  • Gottlieb M, Dweyer DM (1981) Protozoan parasites of humans: surface membrane with externally disposed acid phosphatase. Science 212:939–941

    Article  PubMed  CAS  Google Scholar 

  • Hanna AS, Silva JLM, Giannini MJSM (2000) Adherence and intracellular parasitism of Paracoccidioides brasilienses in Vero cells. Microbiol Infect 2:877–884

    Article  CAS  Google Scholar 

  • Hernandez-Hernandez A, Sanchez-Yague J, Martin-Valmaseda E, Llanillo M (1999) Oxidative inactivation of human and sheep platelet membrane-associated phosphotyrosine phosphatase activity. Free Radic Biol Med 26:1218–1230

    Article  PubMed  CAS  Google Scholar 

  • Hunter T (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80:225–236

    Article  PubMed  CAS  Google Scholar 

  • Huyer G, Liu S, Kelly J, Moffat J, Pavette P, Kennedy B, Tsaprailis G, Gresser MJ, Ramachandran C (1997) Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J Biol Chem 272:843–851

    Article  PubMed  CAS  Google Scholar 

  • Jesus JB, Podlyska TM, Hampshire A, Lopes CS, Vannier-Santos MA, Meyer-fernandes JR (2002) Characterization of an ecto-phosphatase activity in the human parasite Trichomonas vaginalis. Parasitol Res 351:1–16

    Google Scholar 

  • Kneipp LF, Palmeira VF, Pinheiro AAS, Alviano CS, Rozental S, Travassos LR, Meyer-Fernandes JR (2003) Phosphatase activity on the cell wall of Fonsecaea pedrosoi. Med Mycol 41:469–477

    Article  PubMed  CAS  Google Scholar 

  • Kneipp LF, Rodrigues ML, Holandino C, Esteves FF, Souto-Padrón T, Alviano CS, Travassos LR, Meyer-Fernandes JR (2004) Ecto-phosphatase activity in conidial forms of Fonsecaea pedrosoi is modulated by exogenous phosphate and influences fungal adhesion to mammalian cells. Microbiology 150:3355–3362

    Article  PubMed  CAS  Google Scholar 

  • Lemos AP, de Souza ALF, Pinheiro AAS, Berredo-Pinho M, Meyer-Fernandes JR (2002) Ecto-phosphatase activity on the cell surface of Crithidia deanei. Z Naturforsch 57:500–505

    CAS  Google Scholar 

  • Lima OL, Figueiredo CC, Previato JO, Mendonça-Previato L, Morandi V, Lopes Bezerra LM (2001) Involvment of fungal cell wall components in adhesion of Sporotrix shenckii to human fibronectin. Infect Immun 69:6874–6880

    Article  PubMed  CAS  Google Scholar 

  • Limongi CL, Rozental S, Alviano CS, De Souza W (1997) The influence of surface carbohydrates on the interaction of Fonsecaea pedrosoi with Chinese hamster ovary glycosylation cells. Mycopathologia 138:127–135

    Article  PubMed  CAS  Google Scholar 

  • Lowry HO, Lopez M (1946) The determination of inorganic phosphate in the presence of labile phosphate esters. J Biol Chem 162:421–428

    CAS  Google Scholar 

  • Madhani HD, Fink GR (1998) The control of filamentous differentiation and virulence in fungi. Trends Cell Biol 8:348–353

    Article  PubMed  CAS  Google Scholar 

  • Meyer-Fernandes JR, Dutra PML, Rodrigues CO, Saad-Nehme J, Lopes AHCS (1997) Mg-dependent ecto-ATPase activity in Leishmania tropica. Arch Biochem Biophys 341:40–46

    Article  PubMed  CAS  Google Scholar 

  • Meyer-Fernandes JR, Silva-Neto MAC, Soares MS, Fernandes EC, Vercesi AE, Oliveira MM (1999) Ecto-phosphatse activities on the cell surface of the amastigote forms of Trypanosoma cruzi. Z Naturforsch 54c:977–984

    Google Scholar 

  • Mildner P, RiesB, Barbaric S (1975) Acid phosphatase and adenosine triphosphatase activities in the cell wall of beaker’s yeast. Biochim Biophys Acta 391:67–74

    PubMed  CAS  Google Scholar 

  • Nakagura KH, Tachibana H, Kaneda Y (1985) Alteration of the cell surface acid phosphatase concomitant with morphological transformation in Trypanosoma cruzi. Comp Biochem Physiol 81b:815–817

    Google Scholar 

  • Nielsen HS Jr (1967) Effects of amphotericin B in vitro on perfect and imperfect strains of Allescheria boydii. Appl Microbiol 15:86–91

    PubMed  CAS  Google Scholar 

  • Patterson TF, Andriole VT, Zervos MJ, Therasse D, Kauff-man CA (1990) The epidemiology of pseudallescheriasis complicating transplantation: nosocomial and community–acquired infection. Mycoses 33:297–302

    PubMed  CAS  Google Scholar 

  • Peres-Sampaio CE, Palumbo ST, Meyer-Fernandes JR (2001) An ecto-ATPase activity present in Leishmania tropica stimulated by dextran sulfate. Z Naturforsch 56c:820–825

    Google Scholar 

  • Pinto MR, De Sá ACM, Limongi CL, Rozental S, Santos ALS, Barreto-Bergter E (2004) Involvement of peptidorhamnomannan in the interaction of Pseudallescheria boydii and HEp2 cells. Microbiol Infect 6:1259–1267

    Article  CAS  Google Scholar 

  • Rippon JW (1998) Pseudallescheriasis. In: Rippon JW (ed) Medical mycology, 3rd edn. W. B. Saunders, Philadelphia, pp 651–680

    Google Scholar 

  • Rodrigues CO, Dias PML, Barros FS, Souto-Padrón T, Meyer-Fernandes JR, Lopes AHCS (1999) Platelet-activating factor induction of secreted phosphatase activity in Trypanosoma cruzi. Biochem Biophys Res Commun 266:36–42

    Article  PubMed  CAS  Google Scholar 

  • Stone RL, Dixon JE (1994) Protein-tyrosine phosphatase. J Biol Chem 269:31323–31326

    PubMed  CAS  Google Scholar 

  • Sundstrom P (2002) Adhesion in Candida spp. Cell Microbiol 4:461–469

    Article  PubMed  CAS  Google Scholar 

  • Touati E, Dassa E, Dassa J, Boquet PL (1987) Acid phosphatase (pH 2.5) of Escherichia coli: regulatory characteristics. In: Torriani-Gorini A, Rothman FG, Silver S, Wright A, Yagil E (eds) Microorganisms. American Society for Microbiology, Washinngton, DC, USA, pp 31–40

    Google Scholar 

  • Walton KM, Dixon JE (1993) Protein tyrosine phosphatase. Annu Rev Biochem 62:101–120

    Article  PubMed  CAS  Google Scholar 

  • Zhan X-L, Hong Y, Zhu T, Mitchell AP, Deschenes RJ, Guan K-L (2000) Essential functions of protein tyrosine phosphatase Ptp2 and Ptp3 and Rim 11 tyrosine phosphorylation in Sascharomyces cerevisiae meiosis and sporulation. Mol Biol Cell 11:663–676

    PubMed  CAS  Google Scholar 

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Acknowledgments

We acknowledge Dr. Martha Sorenson (Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro) for recommending needed changes in the English. This work was partially supported by grants from the Brazilian Agencies Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Coordenação de Aperfeiçoamento de Pessoal de Nível superior (CAPES) and Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ). Marcia R. Pinto is recipient of a fellowship from Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)—Grants Nos. 05/02776-0 and 05/56161-6.

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Authors and Affiliations

  1. Instututo de Bioquímica Médica, Universidade Federal do Rio de Janeiro, CCS, bloco H, Cidade Universitária, Rio de Janeiro, RJ, 21941-590, Brazil

    Tina Kiffer-Moreira, Ana Acacia S. Pinheiro, Fabiano F. Esteves & José R. Meyer-Fernandes

  2. Instituto de Microbiologia Prof. Paulo de Góes, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, 21941-590, Brazil

    Márcia R. Pinto, Thais Souto-Padrón & Eliana Barreto-Bergter

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  1. Tina Kiffer-Moreira
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  2. Ana Acacia S. Pinheiro
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  3. Márcia R. Pinto
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Correspondence to José R. Meyer-Fernandes.

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Kiffer-Moreira, T., Pinheiro, A.A.S., Pinto, M.R. et al. Mycelial forms of Pseudallescheria boydii present ectophosphatase activities. Arch Microbiol 188, 159–166 (2007). https://doi.org/10.1007/s00203-007-0232-y

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