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Biochemistry of Enzymatic Pathogenicity Factors

  • Chapter
Human and Animal Relationships

Part of the book series: The Mycota ((MYCOTA,volume 6))

Abstract

Secreted proteinases, lipases, and glycosidases produced by the Eumycota are, by and large, components of a repertoire of exoenzymes which participate in absorptive nutrition. Such hydrolases are characterized by broad substrate specificities. Their secretion is induced by exposure of cells to specific nutritive compounds and modulated by physical factors that characterize the ecological niche in which the fungus proliferates. Certain exoenzymes have also been reported to alter the pH of the microenvironment, a secondary function which contributes to optimization of conditions for fungal growth and sporulation. Fungi that evolved as agents of superficial or deep-seated mycoses of mammals have encountered an abundance of proteins, such as keratin, elastin, collagen, albumin, hemoglobin, and immunoglobulins.

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References

  • Abdel-Meguid SS (1993) Inhibitors of aspartyl proteinases. Med Res Rev 13:731–778

    Article  PubMed  CAS  Google Scholar 

  • Agren M, Taplin J, Woessner JF, Eaglstein WH, Merty PM (1992) Collagenase in wound healing: effect of wound age and type. J Invest Dermatol 99:709–714

    Article  PubMed  CAS  Google Scholar 

  • Anaissie E (1992) Opportunistic mycoses in the immunocompromised host: experience at a cancer center and review. Clin Infect Dis 14(Suppl 1): S43–S53

    Article  Google Scholar 

  • Andrews RK, Blakeley RL, Zerner B (1984) Urea and urease. In: Eichhorn GL, Marzilli LG (eds) Advances in organic chemistry, vol 6. Elsevier, New York, pp 245–283

    Google Scholar 

  • Azaryan AV, Wong M, Friedman TC, Cawley NX, Estivariz FE, Chen H-C, Loh YP (1993) Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. J Biol Chem 268:11968–11975

    PubMed  CAS  Google Scholar 

  • Azghani AD, Connelly JC, Peterson BT, Gray LD, Collins ML, Johnson AR (1990) Effects of Pseudomonas aeruginosa elastase on alveolar epithelial permeability in guinea pigs. Infect Immun 58:433–438

    PubMed  CAS  Google Scholar 

  • Baird ML, Garber ED (1981) The genetics and biochemistry of urease in Ustilago violacea. Biochem Genet 9:1101–1114

    Article  Google Scholar 

  • Banerjee A, Ganesan- K, Datta A (1991) Induction of secretory acid proteinase in Candida albicans. J Gen Microbiol 137:2455–2461

    Article  PubMed  CAS  Google Scholar 

  • Banno Y, Yamada T, Nozawa Y (1985) Secreted phospholipases of the dimorphic fungus, Candida albicans: separation of three enzymes and some biological properties. Sabouraudia 23:47–54

    Article  PubMed  CAS  Google Scholar 

  • Barrett-Bee K, Hayes Y, Wilson PG, Ryley J (1985) A comparison of phospholipase activity, cellular adherence and pathogenicity of yeasts. J Gen Microbiol 131:1217–1221

    PubMed  CAS  Google Scholar 

  • Bava AJ, Negroni R, Bianchi M (1993) Cryptococcosis produced by a urease negative strain of Cryptococcus neoformans. J Med Vet Mycol 31:87–89

    Article  PubMed  CAS  Google Scholar 

  • Beveridge AJ, Heywood GC (1993) A quantum mechanical study of the active site of aspartic proteinases. Biochemistry 32:3325–3333

    Article  PubMed  CAS  Google Scholar 

  • Blakeley RL, Zerner B (1984) Jack bean urease: the first nickel enzyme. J Mol Catal 23:263–292

    Article  CAS  Google Scholar 

  • Blanchard A (1990) Ureaplasma urealyticum urease genes: use of a UGA tryptophan codon. Mol Microbiol 4: 669–676

    Article  PubMed  CAS  Google Scholar 

  • Borg M, Rüchel R (1988) Expression of extracellular acid proteinase by proteolytic Candida spp. during experimental infection of oral mucosa. Infect Immun 56: 626–631

    PubMed  CAS  Google Scholar 

  • Borg M, Rüchel R (1990) Demonstration of fungal proteinase during phagocytosis of Candida albicans and Candida tropicalis. J Med Vet Mycol 28:3–14

    Article  PubMed  CAS  Google Scholar 

  • Bouchara J-P, Larcher G, Joubaud F, Penn P, Tronchin G, Chabasse D (1993) Extracellular fibrinogenolytic enzyme of Aspergillus fumigatus: substrate-dependent variations in the proteinase synthesis and characterization of the enzyme. FEMS Immunol Med Microbiol 7:81–92

    Article  PubMed  CAS  Google Scholar 

  • Brady CE, Hadfield TL, Hyatt JR, Utts SJ (1986) Compylobacter pyloridis survival in a hostile environment. Am J Gasteroenterol 81:855

    Google Scholar 

  • Brumlik MJ, Storey DG (1992) Zinc and iron regulate translation of the gene encoding Pseudomonas aeruginosa elastase. Mol Microbiol 6:337–344

    Article  PubMed  CAS  Google Scholar 

  • Bump WS (1925) Observations on growth of Coccidioides immitis. J Infect Dis 36:561–565

    Article  Google Scholar 

  • Calera JA, López-Medrano R, Ovejero MC, Puente P, Leal F (1994) Variability of Aspergillus nidulans antigens with media and time and temperature of growth. Infect Immun 62:2322–2333

    PubMed  CAS  Google Scholar 

  • Capobianco JO, Lerner CG, Goldman RC (1992) Application of a fluorogenic substrate in the assay of proteolytic activity and in the discovery of a potent inhibitor of Candida albicans aspartic proteinase. Anal Biochem 204:96–102

    Article  PubMed  CAS  Google Scholar 

  • Clark PA, Wilcox DE (1989) Magnetic properties of the nickel enzymes urease, nickel-substituted carboxypep-tidase A, and nickel-substituted carbonic anhydrase. Inorg Chem 28:1326–1333

    Article  CAS  Google Scholar 

  • Clark PA, Wilcox DE, Scott RA (1990) X-ray absorption spectroscopic evidence for binding of the competitive inhibitor 2-mercaptoethanol to the nickel sites of jack bean urease. A new Ni-Ni interaction in the inhibited enzymes. Inorg Chem 29:579–581

    Article  CAS  Google Scholar 

  • Cole GT (1993) C. immitis: resistance to host defense mechanisms. Clin Adv in Treatment Fungal Infect 4:1–5, 11–13

    Google Scholar 

  • Cole GT, Seshan KR, Phaneuf M, Lynn KT (1991) Chlamydospore-like cells of Candida albicans in the gastrointestinal tract of infected, immunocompromised mice. Can J Microbiol 37:637–646

    Article  PubMed  CAS  Google Scholar 

  • Cole GT, Seshan KR, Lynn KT, Franco M (1993) Gastrointestinal candidiasis: histopathology of Candida-host interactions in a murine model. Mycol Res 4:385–408

    Article  Google Scholar 

  • Cole GT, Seshan KR, Phaneuf M, Lynn KT (1991) Chlamydospore-like cells of Candida albicans in the gastrointestinal tract of infected, immunocompromised mice. Can J Microbiol 37:637–646

    Article  PubMed  CAS  Google Scholar 

  • Cole GT, Lynn KT, Seshan KR, Pope LM (1989) Gastrointestinal and systemic candidosis in immunocompromised mice. J Med Vet Mycol 27:363–380

    Article  PubMed  CAS  Google Scholar 

  • Costa AL, Misefari A, Amato A (1967) Enzymatic activities of mycetes. 1. Enzymatic acitivty of Candida albicans in egg yolk-containing media. Abstr XIVth Congresso Nazionale di Microbiologia, Messina Taorina

    Google Scholar 

  • Coulot P, Bouchara J-P, Renier G, Annaix V, Planchenault C, Tronchin G, Chabasse D (1994) Specific interaction of Aspergillus fumigatus with fibrinogen and its role in cell adhesion. Infect Immun 62:2169–2177

    PubMed  CAS  Google Scholar 

  • Crandall M, Edwards JE (1987) Segregation of proteinase-negative mutants from heterozygous Candida albicans. J Gen Microbiol 133:2817–2824

    PubMed  CAS  Google Scholar 

  • Creaser EH, Porter RL (1985) The purification of urease from Aspergillus nidulans. Int J Biochem 17:1339–1341

    Article  PubMed  CAS  Google Scholar 

  • Cutfield S, Marshall C, Moody P, Sullivan P, Cutfield J (1993) Crystallization of inhibited asparitc proteinase from Candida albicans. J Mol Biol 234:1266–1269

    Article  PubMed  CAS  Google Scholar 

  • Cutler JE, Brawner DL, Hazen KC, Jutila MA (1990) Characteristics of Candida albicans adherence to mouse tissues. Infect Immun 58:1902–1908

    PubMed  CAS  Google Scholar 

  • Davidson JM (1987) Elastin: structure and biology. In: Uitto J, Perejda AJ (eds) Connective tissue disease: molecular pathology of the extracellular matrix. Marcel Dekker, New York, pp 29–54

    Google Scholar 

  • Davies DR (1990) The structure and function of the aspartic proteinases. Annu Rev Biophys Chem 19: 189–215

    Article  CAS  Google Scholar 

  • DeBernardis F, Lorenzini R, Verticchio R, Agatensi L, Cassone A (1989) Isolation, acid proteinase secretion, and experimental pathogenicity of Candida parapsilosis from outpatients with vaginitis. J Clin Microbiol 27: 2598–2603

    PubMed  Google Scholar 

  • DeBernardis F, Agatensi L, Ross IK, Emerson GW, Lorenzini R, Sullivan PA, Cassone A (1990a) Evidence for a role for secreted aspartate proteinase of Candida albicans in vulvovaginal candidiasis. J Infect Dis 161: 1276–1283

    Article  PubMed  Google Scholar 

  • DeBernardis F, Morelli L, Ceddia T, Lorenzini R, Cassone A (1990b) Experimental pathogenicity and acid proteinase secretion of vaginal isolates of Candida parapsilosis. J Med Vet Mycol 28:125–137

    Article  PubMed  Google Scholar 

  • Denning DW, Ward PN, Fenelon LE, Benbow EW (1992) Lack of vessel wall elastolysis in human invasive pulmonary aspergillosis. Infect Immun 60:5153–5156

    PubMed  CAS  Google Scholar 

  • Denning DW, Elliott J, Keaney M (1993) Temperature-dependent expression of elastase in Aspergillus species. J Med Vet Mycol 31:455–458

    Article  Google Scholar 

  • De Viragh PA, Sanglard D, Togni G, Falchetto R, Monod M (1993) Cloning and sequencing of two Candida parapsilosis genes encoding acid proteases. J Gen Microbiol 139:335–342

    Article  PubMed  Google Scholar 

  • Dixon NE, Gazzola C, Blakeley RL, Zerner B (1975) Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel? J Am Chem Soc 97: 4131–4133

    Article  PubMed  CAS  Google Scholar 

  • Edison AM, Manning-Zweerrink M (1988) Comparison of the extracellular proteinase activity produced by a low virulence mutant of Candida albicans and its wild-type parent. Infect Immun 56:1388–1390

    PubMed  CAS  Google Scholar 

  • EUROGAST Study Group (1993) An international association between Helicobacter infection and gastric cancer. Lancet 341:1359–1362

    Article  Google Scholar 

  • Frey CL, Drutz DJ (1986) Influence of fungal surface components on the interaction of Coccidioides immitis with polymophonuclear neutrophils. J Infect Dis 153: 933–943

    Article  PubMed  CAS  Google Scholar 

  • Frosco M, Chase T, Macmillan JD (1992) Purification and properties of the elastase from Aspergillus fumigatus. Infect Immun 60:728–734

    PubMed  CAS  Google Scholar 

  • Fruton JS (1987) Aspartyl proteinases. In: Neuberger A., Brocklehurst K (eds) Hydrolytic enzymes. Elsevier, Amsterdam, pp 1–37

    Chapter  Google Scholar 

  • Fusek M, Smith EA, Monod M, Foundling SI (1993) Candida parapsilosis expresses and secretes two aspartic proteinases. FEBS Lett 327:108–112

    Article  PubMed  CAS  Google Scholar 

  • Ganesan K, Banerjee A, Datta A (1991) Molecular cloning of the secretory acid proteinase gene from Candida albicans and its use as a species-specific probe. Infect Immun 59:2972–2977

    PubMed  CAS  Google Scholar 

  • Ghannoum M, Elteen KA (1986) Corelative relationship between proteinase production, adherence and pathogenicity of various strains of Candida albicans. J Med Vet Mycol 24:407–413

    Article  PubMed  CAS  Google Scholar 

  • Ghannoum MA, Filler SG, Ibrahim AS, Fu Y, Edwards JE (1992) Modulation of interactions of Candida albicans and endothelial cells by fluconazole and amphotericin B. Antimicrob Agents Chemother 36:2239–2288

    Article  PubMed  CAS  Google Scholar 

  • Gilleland HE, Gilleland LB, Fowler MR (1993) Vaccine efficacies of elastase, exotoxin A, and outermembrane protein F in preventing chronic pulmonary infection by Pseudomonas aeruginosa in a rat model. J Med Microbiol 38:79–86

    Article  PubMed  CAS  Google Scholar 

  • Goldman RC, Capobianco JO (1994) Detection of Candida spp. secreted aspartyl protease in biological fluids using a sensitive fluorogenic peptide substrate. Abstr P05.7, Int Soc Human Animal Mycoses Congr, Adelaide, Australia, pD128

    Google Scholar 

  • Graham DY, Lew GM, Klein PD, Evans DG, Evans DJ, Saeed ZA, Malaty HM (1992) Effect of treatment of Helicobacter pylori infection on the long-term recurrence of gastric or duodenal ulcer. Ann Intern Med 116:705–708

    PubMed  CAS  Google Scholar 

  • Graham JES, Sodek J, Hofmann T (1973) Rhizopus acid proteinases (Rhizopus-pepsim): properties and homology with other acid proteinases. Can J Biochem 51: 789–796

    Article  PubMed  CAS  Google Scholar 

  • Habermann E, Hardt KL (1972) A sensitive and specific plate test for the quantitation of phospholipases. Anal Biochem 50:163–173

    Article  PubMed  CAS  Google Scholar 

  • Harboe M, Andersen PM, Foltmann B, Kay J, Kassell B (1974) The activation of bovine pepsinogen. J Biol Chem 249:4487–4494

    PubMed  CAS  Google Scholar 

  • Hartley BS (1960) Proteolytic enzymes. Annu Rev Biochem 29:45–72

    Article  PubMed  CAS  Google Scholar 

  • Hattori M, Yoshiura K, Negi M, Ogawa H (1984) Keratinolytic proteinase produced by Candida albicans. Sabouraudia 22:175–183

    Article  PubMed  CAS  Google Scholar 

  • Hazell SL, Lee A (1986) Campylobacter pyloridis, urease, hydrogen ion back diffusion, and gastric ulcers. Lancet 2:15–17

    Article  PubMed  CAS  Google Scholar 

  • Homma M, Kanbe T, Chibana H, Tanaka K (1992) Detection of intracellular forms of secretory aspartic proteinase in Candida albicans. J Gen Microbiol 138:627–633

    Article  PubMed  CAS  Google Scholar 

  • Hornebeck W, Brechemier D, Jacob MP, Frances C, Robert L (1984) On the multiplicity of cellular elastases and their inefficient control by natural inhibitors. In: Hörl WH, Heidland A (eds) Proteases: potential role in health and disease. Plenum Press, New York, pp 111–119

    Google Scholar 

  • Hube B, Turver CJ, Odds FC, Eiffert H, Boulnois GJ, Köchel H, Rüchel R (1991) Sequence of the Candida albicans gene encoding the secretory aspartate proteinase. J Med Vet Mycol 29:129–132

    Article  PubMed  CAS  Google Scholar 

  • Hube B, Monod M, Schofield DA, Brown AJP, Gow NAR (1994) Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicans. Mol Microbiol 14:87–99

    Article  PubMed  CAS  Google Scholar 

  • Ibrahim AS, Filler SG, Ghannoum MA, Edwards JE(1993) Interferon-gamma protects endothelial cells from damage by Candida albicans. J Infect Dis 167: 1467–1470

    Article  PubMed  CAS  Google Scholar 

  • Ibrahim AS, Mirbod F, Filler SG, Banno Y, Cole GT, Kitajima Y, Edwards JE, Nozawa Y, Ghannoum MA (1995) Evidence implicating phospholipase as a virulence factor in Candida albicans Infect Immun 63:1993–1998

    PubMed  CAS  Google Scholar 

  • Ishii T, Fukushima J, Fujita S, Shigematsu T, Ando N, Ishiwata T, Kurata M, Kawamoto S, Morihara K, Okuda K (1994) Elastase gene expression in non-elastase producing Pseudomonas aeruginosa strains using novel shuttle vector systems. FEMS Microbiol Lett 116: 307–314

    Article  PubMed  CAS  Google Scholar 

  • Jarai G, Buxton FP (1994) Cloning and characterization of the pepD gene of Aspergillus niger which codes for a subtilisin-like protease. Gene 139:51–57

    Article  PubMed  CAS  Google Scholar 

  • Jaton-Ogay K, Suter M, Crameri R, Falchetto R, Fatih A, Monod M (1992) Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus. FEMS Microbiol Lett 92:163–168

    Article  CAS  Google Scholar 

  • Jaton-Ogay K, Paris S, Huerre M, Quadroni M, Falchetto R, Togni G, Large JP, Monod M (1994) Cloning and disruption of the gene encoding an extracellular metal-loprotease of Aspergillus fumigatus. Mol Microbiol 14: 917–928

    Article  PubMed  CAS  Google Scholar 

  • Jiang W, Bond JS (1992) Families of metallopeptidases and their relationship. FEBS Lett 312:110–114

    Article  PubMed  CAS  Google Scholar 

  • Kaltwasser H, Schlegel HG (1966) NADH-dependent coupled assay for urease and other ammonia-producing systems. Anal Biochem 16:132–138

    Article  PubMed  CAS  Google Scholar 

  • Kaminishi H, Hagihara Y, Hayashi S, Cho T (1986) Isolation and characteristics of collagenolytic enzyme produced by Candida albicans. Infect Immun 53: 312–316

    PubMed  CAS  Google Scholar 

  • Kaminishi H, Hagihara Y, Tamaka M, Cho T (1988) Degradation of bovine achules tendon collagen by Candida albicans proteinase. J Med Vet Mycol 26: 315–318

    Article  PubMed  CAS  Google Scholar 

  • Karam GH, Griffin FM (1986) Invasive pulmonary aspergillosis in immunocompromised non-neutropenic hosts. Rev Infect Dis 8:357–363

    Article  PubMed  CAS  Google Scholar 

  • Knipp U, Birkholz S, Kaup W, Mahnke K, Opferkuch W (1994) Suppression of human mononuclear cell response by Helicobacter pylori: effects on isolated monocytes and lymphocytes. FEMS Immunol Med Microbiol 8: 157–166

    Article  PubMed  CAS  Google Scholar 

  • Kobashi K, Takebe S, Numata A (1985) Specific inhibition of urease by N-acylphosphoric triamides. J Biochem 98:1681–1688

    PubMed  CAS  Google Scholar 

  • Kobayashi H, Kusakabe I, Murakami K (1985) Purification and characterization of pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus). Agric Biol Chem 49:2393–2397

    Article  CAS  Google Scholar 

  • Kolattukudy PE, Lee JD, Rogers LM, Zimmerman P, Ceselski S, Fox B, Stein B, Copelan EA (1993) Evidence for possible involvement of an elastolytic serine protease in aspergillosis. Infect Immun 61:2357–2368

    PubMed  CAS  Google Scholar 

  • Kothary MH, Chase T, Macmillan JD (1984) Correlation of elastase production by some strains of Aspergillus fumigatus with ability to cause pulmonary invasive aspergillosis in mice. Infect Immun 43:320–325

    PubMed  CAS  Google Scholar 

  • Kregar I, Urh I, Umezawa H, Turk V (1977) Purification of cathepsin D by affinity chromatography on pepstatin Sepharose column. Croat Chem Acta 49:587–592

    CAS  Google Scholar 

  • Kunert J (1987) Utilization of various concentrations of free cystine by the fungus Microsporum gypseum. J Basic Microbiol 27:207–213

    Article  PubMed  CAS  Google Scholar 

  • Kunert J (1989) Biochemical mechanisms of keratin degradation by actinomycete Streptomyces fradiae and fungus Microsporum gypseum: a comparison. J Basic Microbiol 29:597–604

    Article  CAS  Google Scholar 

  • Kuzmic P, Sun CO, Zhao ZC, Rich DH (1991) Nospecific electrostatic binding of substrates and inhibitors to porcine pepsin. In: Dunn BM (ed) Structure and function of the aspartic porteinases: genetics, structures, and mechanisms. Plenum Press, New York, pp 75–86

    Chapter  Google Scholar 

  • Kwon-Chung KJ, Bennett JE (1992) Aspergillosis and cryptococcosis. In: Kwon-Chung KJ, Bennett JE (eds) Medical mycology. Lea and Febiger, Philadelphia, pp 201–247, pp 397–446

    Google Scholar 

  • Kwon-Chung KJ, Lehman D, Good C, Magee PT (1985) Genetic evidence for role of extracellular proteinase in virulence of Candida albicans. Infect Immun 49:571–575

    PubMed  CAS  Google Scholar 

  • Lam M, Peterkin V, Reiss E, Morrison CJ (1991) Effect of growth conditions on the extracellular production of the aspartic proteinase of Candida albicans. In: Dunn BM (ed) Structure and function of the aspartic proteinases: genetics, structures, and mechanisms. Plenum Press, New York, pp 265–267

    Chapter  Google Scholar 

  • Larcher G, Bouchara J-P, Annaix V, Symoens F, Chabasse D, Tronchin G (1992) Purification and characterization of a fibrinogenolytic serine proteinase from Aspergillus fumigatus culture filtrate. FEBS Lett 308:65–69

    Article  PubMed  CAS  Google Scholar 

  • Lerner CG, Goldman RC (1993) Stimuli that induce production of Candida albicans extracellular aspartyl proteinase. J Gen Microbiol 139:1643–1651

    Article  PubMed  CAS  Google Scholar 

  • Li A, Guo N, Wu S (1993) A strain of urease-negative Cryptococcus neoformans isolated from the environment in China. Chin Med Sci J 8:52–54

    PubMed  CAS  Google Scholar 

  • Lin X, Wong RNS, Tang J (1989) Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen. J Biol Chem 264:4482–4489

    PubMed  CAS  Google Scholar 

  • Lott TJ, Page LS, Boiron P, Benson J, Reiss E (1989) Nucleotide sequence of the Candida albicans aspartyl proteinase gene. Nucleic Acids Res 17:1779

    Article  PubMed  CAS  Google Scholar 

  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    PubMed  CAS  Google Scholar 

  • MacDonald F (1984) Secretion of inducible proteinase by pathogenic Candida species. Sabouraudia 22:79–82

    Article  PubMed  CAS  Google Scholar 

  • MacDonald F, Odds FC (1983) Virulence for mice of a proteinase secreting strain of Candida albicans and a proteinase-deficient mutant. J Gen Microbiol 129: 431–438

    PubMed  CAS  Google Scholar 

  • Mackay EM, Pateman JA (1980) Nickel requirement of a urease-deficient mutant in Aspergillus nidulans. J Gen Microbiol 116:249–251

    PubMed  CAS  Google Scholar 

  • Mackay EM, Pateman JA (1982) The regulation of urease activity in Aspergillus nidulans. Biochem Genet 20: 763–776

    Article  PubMed  CAS  Google Scholar 

  • Magee BB, Hube B, Wright RJ, Sullivan PA, Magee PT (1993) The genes encoding the secreted aspartyl proteinases of Candida albicans constitute a family with at least three members. Infect Immun 61:3240–3242

    PubMed  CAS  Google Scholar 

  • Malviya HK, Rajak RC, Hasija SK (1992a) Purification and partial characterization of extracellular keratinases of Scopulariopsis brevicaulis. Mycopathologia 119: 161–165

    Article  PubMed  CAS  Google Scholar 

  • Malviya HK, Rajak RC, Hasija SK (1992b) Synthesis and regulation of extracellular keratinases in three fungi isolated from the grounds of a gelatin factory, Jabalfur, India. Mycopathologia 120:1–4

    Article  CAS  Google Scholar 

  • Maresca B, Carratù L (1992) The biology of the heat shock response in parasites. Parasitol Today 8:260–266

    Article  PubMed  CAS  Google Scholar 

  • Maresca B, Carratù L, Kobayashi GS (1994) Morphologic transition in the human fungal pathogen Histoplasma capsulatum. Trends Microbiol 8:260–266

    Google Scholar 

  • Markaryan A, Morozova I, Yu H, Kolattukudy PE (1994) Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and im-munoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung. Infect Immun 62:2149–2157

    PubMed  CAS  Google Scholar 

  • Matthews BW, Colman PM, Jansonius JN, Titani K, Walsh KA, Neurath H (1972a) Structure of thermolysin. Nature (Lond) New Biol 238:41–43

    Article  CAS  Google Scholar 

  • Matthews BW, Jansonius JN, Colman PM, Schoenborn BP, Dupourque D (1972b) Three-dimensional structure of thermolysin. Nature (Lond) New Biol 238:37–41

    Article  CAS  Google Scholar 

  • Millner OE, Andersen JA, Appier ME, Benjamin CE, Edwards JG, Humphrey DT, Shearer EM (1982) Flurofamide: a potent inhibitor of bacterial urease with potential clinical utility in the treatment of infection induced urinary stones. J Urol 127:346–350

    PubMed  CAS  Google Scholar 

  • Mirbod F, Banno Y, Ghannoum MA, Ibrahim AS, Nakashima S, Kitajima Y, Cole GT, Nozawa Y (1995) Purification and characterization of lysophospholipase-transacylace (h-LPTA) from a highly virulent strain of Candida albicans. Biochim Biophys Acta (in press)

    Google Scholar 

  • Miyasaki SH, White TC, Agabian N (1994) A fourth secreted aspartyl proteinase gene (SAP4) and a CARE2 repetitive element are located upstream of the SAP1 gene in Candida albicans. J Bacteriol 176:1702–1710

    PubMed  CAS  Google Scholar 

  • Mobley HLT, Hausinger RP (1989) Microbial ureases: significance, regulation, and molecular characterization. Microbiol Rev 53:85–108

    PubMed  CAS  Google Scholar 

  • Mobley HLT, Jones BD, Jerse AE (1986) Cloning of urease gene sequence from Providencia stuartii. Infect Immun 54:161–169

    PubMed  CAS  Google Scholar 

  • Monod M, Togni G, Rahalison L, Frenk E (1991) Isolation and characterization of an extracellular alkaline protease of Aspergillus fumigatus. J Med Microbiol 35: 23–28

    Article  PubMed  CAS  Google Scholar 

  • Monod M, Paris S, Sanglard D, Jaton-Ogay K, Bille J, Latgé J-P (1993a) Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus. Infect Immun 61:4099–4104

    PubMed  CAS  Google Scholar 

  • Monod M, Paris S, Sarfati J, Jaton-Ogay K, Ave P, Latgé J-P (1993b) Virulence of alkaline-protease-deficient mutants of Aspergillus fumigatus. FEMS Microbiol Lett 106:39–46

    Article  PubMed  CAS  Google Scholar 

  • Monod M, Togni G, Hube B, Sanglard D (1994) Multiplicity of genes encoding secreted aspartic proteinases in Candida species. Mol Microbiol 13:357–368

    Article  PubMed  CAS  Google Scholar 

  • Monod M, Fatih A, Jaton-Ogay K, Paris S, Latgé J-P (1995) The secreted proteases by pathogenic species of Aspergillus and their questionable role in virulence. Can J Bot 73(Suppl 1): S1081–S1086

    Article  Google Scholar 

  • Montalvo JG (1970) An improved urease electrode. Anal Biochem 38:357–363

    Article  PubMed  CAS  Google Scholar 

  • Morihara K, Tsuzuki HT (1971) Comparative study of various neutral proteinases from microorganisms: specificity with oligopeptides. Arch Biochem Biophys 146: 291–296

    Article  PubMed  CAS  Google Scholar 

  • Morrison CJ, Hurst SF, Bragg SL, Kuykendall RJ, Diaz H, McLaughlin DW, Reiss E (1993a) Purification and characterization of the extracellular aspartyl proteinase of Candida albicans: removal of extraneous proteins and cell wall mannoprotein and evidence for lack of glycosylation. J Gen Microbiol 139:1177–1186

    Article  PubMed  CAS  Google Scholar 

  • Morrison CJ, Hurst SF, Bragg SL, Kuykendall RJ, Diaz H, Pohl J, Reiss E (1993b) Heterogeneity of the purified extracellular aspartyl proteinase from Candida albicans. Characterization with monoclonal antibodies and N-terminal amino acid sequence analysis. Infect Immun 61:2030–2036

    PubMed  CAS  Google Scholar 

  • Morrow B, Srikantha T, Soll DR (1992) Transcription of the gene for a pepsinogen, PEP1, is regulated by white-opaque switching in Candida albicans. Mol Cell Biol 12:2997–3005

    PubMed  CAS  Google Scholar 

  • Moser M, Menz G, Blaser K, Crameri R (1994) Recombinant expression and antigenic properties of a 32-kilodalton extracellular alkaline protease, representing a possible virulence factor from Aspergillus fumigatus. Infect Immun 62:936–942

    PubMed  CAS  Google Scholar 

  • Moutaouakil MN, Monod M, Prévost MC, Bouchara J-P, Paris S, Latgé J-P (1993) Identification of the 33-kDa alkaline protease of Aspergillus fumigatus in vitro and in vivo. J Med Microbiol 39:393–399

    Article  PubMed  CAS  Google Scholar 

  • Mukai H, Takeda O, Asada K, Kato I Murayama SY, Yamaguchi H (1992) cDNA cloning of an aspartic proteinase secreted by Candida albicans. Microbiol Immunol 36:1207–1216

    PubMed  CAS  Google Scholar 

  • Murayama S Y (1993) cDNA cloning of Candida albicans aspartic proteinase and its diagnostic application. In: Maresca B, Kobayashi GS, Yamaguchii H (eds) Molecular biology and its application to medical mycology. NATO ASI Series H69. Springer, Berlin Heidelberg New York, pp 149–158

    Chapter  Google Scholar 

  • Nishino N, Powers JC (1980) Pseudomonas aeruginosa elastase. J Biol Chem 255:3482–3486

    PubMed  CAS  Google Scholar 

  • Oda K, Murao S (1991) Pepstatin-insensitive carboxyl proteinases. In: Dunn BM (ed) Structure and function of the aspartic proteinases: genetics, structures, and mechanisms. Plenum Press, New York, pp 185–201

    Chapter  Google Scholar 

  • Odds F (1988) Candida and candidosis, 2nd edn. Balliere Tindall, Philadelphia

    Google Scholar 

  • Odds F (1991) Potential for penetration of passive barriers to fungal invasion in humans. In: Cole GT, Hoch HC (eds) The fungal spore and disease initiation in plants and animals. Plenum Press, New York, pp 287–295

    Google Scholar 

  • Ollert MW, Söhnchen R, Korting HC, Ollert U, Bräutigam S, Bräutigam W (1993) Mechanisms of adherence of Candida albicans to cultured human epidermal kera-tinocytes. Infect Immun 61:4560–4568

    PubMed  CAS  Google Scholar 

  • Pateman JA, Dunn E, Mackay EM (1982) Urea and thiourea transport in Aspergillus nidulans. Biochem Genet 20:777–790

    Article  PubMed  CAS  Google Scholar 

  • Perfect JR, Toffaletti DL, Rude TH (1993) The gene encoding phosphoribosylaminoimidazole carboxylase (ADE2) is essential for growth of Cryptococcus neoformans in cerebrospinal fluid. Infect Immun 61:4446–4451

    PubMed  CAS  Google Scholar 

  • Poulter R, Jeffery K, Hubbard MJ, Shepherd MG, Sullivan PA (1981) Parasexual genetic analysis of Candida albicans by spheroplast fusion. J Bacteriol 146:833–840

    PubMed  CAS  Google Scholar 

  • Price MF, Cawson RA (1977) Phospholipase activity in Candida albicans. Sabouraudia 15:179–185

    Article  PubMed  CAS  Google Scholar 

  • Price MF, Wilkinson ID, Gentry LO (1982) Plate method for detection of phospholipase activity in Candida albicans. Sabouraudia 20:7–14

    Article  PubMed  CAS  Google Scholar 

  • Pugh D, Cawson RA (1975) The cytochemical localization of phospholipase A and lysophospholipase in Candida albicans. Sabouraudia 13:110–115

    Article  PubMed  Google Scholar 

  • Pugh D, Cawson RA (1977) The cytochemical localization of phospholipase in Candida albicans infecting the chick chorio-allantoic membrane. Sabouraudia 15:29–35

    Article  PubMed  CAS  Google Scholar 

  • Rajak RC, Parwekar S, Malviva HK, Hasija SK (1991) Keratin degradation by fungi isolated from the grounds of a gelatin factory campus in Jabalpur, India. Myco-pathologia 114:83–87

    CAS  Google Scholar 

  • Rajak RC, Malviya HD, Deshpande H, Hasija SK (1992) Keratinolysis by Absidia cylindrospora and Rhizomucor pusillus: biochemical proof. Mycopathologia 118: 109–114

    Article  PubMed  CAS  Google Scholar 

  • Ramesh MV, Sirakova T, Kolattukudy PE (1994) Isolation, characterization, and cloning of cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus. Infect Immun 62:79–85

    PubMed  CAS  Google Scholar 

  • Ravdin JI, Murphy CF, Guerrant RL, Long-Krug SA (1985) Effect of antagonists of calcium and phospholipase A on the cytopathogenicity of Entamoeba histolytica. J Infect Dis 152:542–549

    Article  PubMed  CAS  Google Scholar 

  • Ray TL, Payne CD (1988) Scanning electron microscopy of epidermal adherence and cavitation in murine candidiasis: a role for Candida acid proteinase. Infect Immun 56:1942–1949

    PubMed  CAS  Google Scholar 

  • Ray TL, Payne CD (1990) Comparative production and rapid purification of Candida acid proteinase from protein-supplemented cultures. Infect Immun 58: 508–514

    PubMed  CAS  Google Scholar 

  • Ray TL, Payne CD (1991) Degradation of basement membrane matrix proteins laminin, fibronectin, and type IV collagen by Candida acid proteinase. J Invest Dermatol 96:606A

    Google Scholar 

  • Ray TL, Payne CD (1994) Role of Candida acid proteinase in adhesion and invasion of murine epidermis. Abstr S5.5, Int Soc Human Animal Mycoses Congr, Adelaide, Australia, pD7

    Google Scholar 

  • Ray TL, Payne CD, Morrow BJ (1991) Candida albicans acid proteinase: characterization and role in candidiasis. In: Dunn BM (ed) Structure and function of the aspartic proteinases: genetics, structures, and mechanisms. Plenum Press, New York, pp 173–183

    Chapter  Google Scholar 

  • Reichard U, Büttner S, Eiffert H, Staib F, Rüchel R (1990) Purification and characterization of an extracellular serine proteinase from Aspergillus fumigatus and its detection in tissue. J Med Microbiol 33:243–251

    Article  PubMed  CAS  Google Scholar 

  • Reichard M, Eiffert H, Rüchel R (1994) Purification and characterization of an extracellular aspartic proteinase from Aspergillus fumigatus. J Med Vet Mycol 32:427–436

    Article  PubMed  CAS  Google Scholar 

  • Reiss E (1986) Molecular immunology of mycotic and actinomycotic infections. Elsevier, New York

    Google Scholar 

  • Remold H, Fasold H, Staib F (1968) Purification and characterization of a proteolytic enzyme from Candida albicans. Biochim Biophys Acta 167:399–406

    Article  PubMed  CAS  Google Scholar 

  • Rhodes JC (1995) Aspergillus proteinases and their interactions with host tissues. Can J Bot 73(Suppl 1): S1126–S1131

    Article  Google Scholar 

  • Rhodes J, Amlung TW (1990) Elastase-deficient Aspergillus flavus has reduced virulence in mice. Abstr F-31, 90th Annu Meet Soc Microbiol, Anaheim, California, 413 pp

    Google Scholar 

  • Rhodes JC, Amlung TW (1991) The elastinolytic proteinase of Aspergillus flavus is not glycosylated. J Med Vel Mycol 29:407–411

    Article  CAS  Google Scholar 

  • Rhodes JC, Bode RB, McCuan-Kirsch CM (1988) Elastase production in clinical isolates of Aspergillus. Diag Microbiol Infect Dis 10:165–170

    Article  CAS  Google Scholar 

  • Rhodes JC, Amlung TW, Miller MS (1990) Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus. Infect Immun 58:2529–2534

    PubMed  CAS  Google Scholar 

  • Riddles PW, Whan V, Blakeley RL, Zenner B (1991) Cloning and sequencing of a jack bean urease-encoding cDNA. Gene 108:265–267

    Article  PubMed  CAS  Google Scholar 

  • Rippon JW, Varadi DP (1968) The elastases of pathogenic fungi and actinomycetes. J Invest Dermatol 50:54–58

    PubMed  CAS  Google Scholar 

  • Ross IK, DeBernardis F, Emerson GW, Gassone A, Sullivan PA (1990) The secreted aspartate proteinase of Candida albicans: physiology of secretion and virulence of a proteinase-deficient mutant. J Gen Microbiol 136: 687–694

    Article  PubMed  CAS  Google Scholar 

  • Rüchel R (1981) Properties of a purified proteinase from the yeast Candida albicans. Biochim Biophys Acta 659: 99–113

    Article  PubMed  Google Scholar 

  • Rüchel R (1986) Cleavage of immunoglobulins by pathogenic yeasts of the genus Candida. Microbiol Sci 3: 316–319

    PubMed  Google Scholar 

  • Rüchel R, Trost M (1981) A study of the structural conversions of two carboxyl proteinases employing electrophoresis across a pH gradient. In: Allen RC, Amand P (eds) Electrophoresis ’81. de Gruyter Berlin, pp 667–676

    Google Scholar 

  • Rüchel R, Tegeler R, Trost M (1982) A comparison of secretory proteinases from different strains of Candida albicans. Sabouraudia 20:233–244

    Article  PubMed  Google Scholar 

  • Rüchel R, Uhlemann K, Böning B (1983) Secretion of acid proteinases by different species of the genus Candida. Zentralbl Bakt Hyg I Abt Drig A 255:537–548

    Google Scholar 

  • Rüchel R, Böning B, Jahn E (1985) Identification and partial characterization of two proteinases from the cell envelope of Candida albicans blastospores. Zentralbl Bakt Hyg A 260:523–538

    Google Scholar 

  • Rüchel R, Böning B, Borg M (1986) Characterization of a secretory proteinase of Candida parapsilosis and evidence for the absence of the enzyme during infection in vitro. Infect Immun 53:411–419

    PubMed  Google Scholar 

  • Rüchel R, DeBernardis F, Ray TL, Sullivan PA, Cole GT (1992) Candida acid proteinases. J Med Vet Mycol 30(Suppl 1):123–132

    Article  PubMed  Google Scholar 

  • Rüchel R, Olschewski K, Hube B (1994a) Extracellular proteolytic activity of Candida glabrata. Abstr P01.16, Int Sot Human Animal Mycoses Congr, Adelaide, Australia, pD56

    Google Scholar 

  • Rüchel R, Seshan KR, Cole GT (1994b) pH correlates between endosporulating spherules and tissue abscesses. Abstr Centennial Conf on Coccidioidomycosis, San Jose, California

    Google Scholar 

  • Rust L, Messing CR, Iglewski BH (1994) Elastase assays. In: Clark VL, Bavoil PM (eds) Methods in enzymology, vol 235. Bacterial pathogenesis, part A. Identification and regulation of virulence factors. Academic Press, New York, pp 554–562

    Google Scholar 

  • Rüchel R, Zimmermann F, Böning B, Helmchen U (1991) Candidiasis visualized by proteinase-directed immunofluorescence. Virchows Archiv Pathol Anat 419:199–202

    Article  Google Scholar 

  • Saffer LD, Schwartzman JD (1991) A soluble phospho-lipase of Toxoplasma gondii associated with host cell penetration. J Protozool 38:454–460

    PubMed  CAS  Google Scholar 

  • Salyers AA, Whitt DD (1994) Bacterial pathogenesis: a molecular approach. American Society for Microbiology Press, Washington, DC, 264 pp

    Google Scholar 

  • Samaranayake LP, Geddes DAM, Weetman DA, Mac-Farlane TW (1983) Growth and acid production of Candida albicans in carbohydrate supplemented media. Microbios 37:105–115

    PubMed  CAS  Google Scholar 

  • Samaranayake LP, Hughes A, MacFarlane TW (1984) Proteolytic potential of Candida albicans in human saliva supplemented with glucose. J Med Microbiol 17:13–22

    Article  PubMed  CAS  Google Scholar 

  • Sanglard D, Togni G, de Viragh PA, Monod M (1992) Disruption of the gene encoding the secreted acid protease (ACP) in the yeast C. tropicalis. FEMS Microbiol Lett 95:149–156

    Article  CAS  Google Scholar 

  • Seifter S, Harper E (1971) The collagenases. In: Boyer PD (ed) The enzymes, vol 3. Academic Press, New York, pp 649–697

    Google Scholar 

  • Shaik-M MB, Guy AL, Pancholy SK (1980) An improved method for the detection and preservation of urease activity in Polyacrylamide gels. Anal Biochem 103: 140–143

    Article  Google Scholar 

  • Shotton DM (1970) Elastase. In: Perlmann GE, Lorand I (eds) Methods in enzymology, Academic Press, New York, pp 113–140

    Google Scholar 

  • Silverman DJ, Santucci LA, Meyers N, Sekeyova ZA (1992) Penetration of host cells by Rickettsia rickettsii appears to be mediated by phospholipase of rickettsial origin. Infect Immun 60:2733–2740

    PubMed  CAS  Google Scholar 

  • Sirakova TD, Markaryan A, Kolattukudy PE (1994) Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloproteinase from Aspergillus fumigatus and its expression in Escherichia coli. Infect Immun 62:4208–4218

    PubMed  CAS  Google Scholar 

  • Smith PT, King AD, Goodman N (1993) Isolation and characterization of urease from Aspergillus niger. J Gen Microbiol 139:957–962

    Article  PubMed  CAS  Google Scholar 

  • Soll DR (1992) High-frequency switching in Candida albicans. Clin Microbiol Rev 5:183–203

    PubMed  CAS  Google Scholar 

  • Spitzer ED, Kobayashi GS (1988) Aspergillus proteinases and aspergillosis. In: Vanden Bossche H, MacKenzie DWR, Cauwenbergh G (eds) Aspergillus and aspergillosis. Plenum Press, New York, pp 129–132

    Google Scholar 

  • Staib F (1965) Serum-proteins as nitrogen source for yeastlike fungi. Sabouraudia 4:187–193

    Article  PubMed  CAS  Google Scholar 

  • Starcher BC(1986) Elastinandthelung. Thorax 41:577–585

    Article  PubMed  CAS  Google Scholar 

  • Stepanov VM, Rudenskaya GN, Yanonis VV, Ostoslav-skaya VI, Gonchar MV, Kotova EK, Strongin AY (1978) Affinity chromatography of proteinases on sorbents containing bacitracin as a specific ligand. Bioorg Khim 4:1256–1263

    CAS  Google Scholar 

  • Sturtevant J, Latgé J-P (1992) Interactions between conidia of Aspergillus fumigatus and human complement component C3. Infect Immun 60:1913–1918

    PubMed  CAS  Google Scholar 

  • Sumner JB (1926) The isolation and crystallization of the enzyme urease. J Biol Chem 69:435–441

    CAS  Google Scholar 

  • Szewczuk Z, Rebholz KL, Rich DH (1992) Synthesis and biological activity of new informationally restricted analogues of pepstatin. Int J Pep Res 40:233–242

    Article  CAS  Google Scholar 

  • Takahashi K, Inoue H, Sakai K, Kohama T, Kitahara S, Takishima K, Tanji M, Athauda SBP, Takahashi T, Akanuma H, Mamiya G, Yamasaki M (1991) The primary structure of Aspergillus niger acid proteinase A. J Biol Chem 266:19480–19483

    PubMed  CAS  Google Scholar 

  • Takahashi M, Banno Y, Nozawa Y (1991) Secreted Candida albicans phospholipases: purification and characterization of two forms of lysophospholipase-transacylase. J Med Vet Mycol 29:193–204

    Article  PubMed  CAS  Google Scholar 

  • Takishima K, Suga T, Mamiya G (1988) The structure of jack bean urease. Eur J Biochem 175:151–165

    Article  PubMed  CAS  Google Scholar 

  • Tamura Y, Suzuki S, Sawada T (1992) Role of elastase as a virulence factor in experimental Pseudomonas aeruginosa infection in mice. Microbiol Pathogen 12: 237–244

    Article  CAS  Google Scholar 

  • Tang CM, Cohen J, Holden DW (1992) An Aspergillus fumigatus alkaline protease mutant constructed by gene disruption is deficient in extracellular elastase activity. Mol Microbiol 6:1663–1671

    Article  PubMed  CAS  Google Scholar 

  • Tang CM, Cohen J, Krausz T, Van Noorden S, Holden DW (1993) The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect Immun 61:1650–1656

    PubMed  CAS  Google Scholar 

  • Tang J (1979) Evolution in the structure and function of carboxyl proteases. Mol Cell Biochem 26:93–109

    Article  PubMed  CAS  Google Scholar 

  • Tang J, Wong RNS (1987) Evolution in the structure and function of aspartic proteases. J Cell Biochem 33:53–63

    Article  PubMed  CAS  Google Scholar 

  • Tang J, James MNG, Hsu IN, Jenkins JA, Blundell TL (1978) Structural evidence for gene duplication in the evolution of the acid proteases. Nature 271:618–621

    Article  PubMed  CAS  Google Scholar 

  • Tatsumi H, Ohsawa M, Tsuji RF, Murakami S, Nakano E, Motai H, Masaki A, Ishida Y, Murakami K, Kawabe H, Arimura H (1988) Cloning and sequencing of the alkaline proteinase cDNA from Aspergillus oryzae. Agric Biol Chem 52:1887–1888

    Article  CAS  Google Scholar 

  • Tatsumi H, Ogawa Y, Murakami S, Ishida Y, Murakami K, Masaki A, Kawabe H, Arimura H, Nakano E, Motai H (1989) A full length cDNA clone for the alkaline protease from Aspergillus oryzae: structural analysis and expression in Saccharomyces cerevisiae. Mol Gen Genet 219:33–38

    Article  PubMed  CAS  Google Scholar 

  • Tatsumi H, Murakami S, Tsuji RF, Ishida Y, Murakami K, Masaki H, Kawabe H, Arimura H, Nakano E, Motai H (1991) Cloning and expression in yeast of a cDNA clone encoding Aspergillus oryzae neutral protease II, a unique metalloprotease. Mol Gen Genet 228:97–103

    Article  PubMed  CAS  Google Scholar 

  • Todd MJ, Hausinger RP (1991) Identification of the essential cysteine residue in Klebsiella aerogenes urease. J Biol Chem 266:24327–24331

    PubMed  CAS  Google Scholar 

  • Togni G, Sanglard D, Falchetto R, Monod M (1991) Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis. FEBS Lett 286:181–185

    Article  PubMed  CAS  Google Scholar 

  • Togni G, Sanglard D, Monod M (1994) Acid proteinase secreted by Candida tropicalis: virulence in mice for a proteinase-negative mutant. J Med Vet Mycol 32: 257–265

    Article  PubMed  CAS  Google Scholar 

  • Tronchin G, Bouchara J-P, Larcher G, Lissitzky J-C, Chabasse D (1993) Interaction between Aspergillus fumigatus and basement membrane laminin: binding and substrate degradation. Biol Cell 77:201–208

    Article  PubMed  CAS  Google Scholar 

  • Tsuboi R, Ogawa H (1994) Comparison of proteinase, lipase and alpha-glucosidase activities from Candida species and their pathogenic roles. Abstr S5.1, Int Soc Human Animal Mycoses Congr, Adelaide, Australia, pD6

    Google Scholar 

  • Tsujita Y, Endo A (1980) Intracellular localization of two molecular forms of membrane acid proteinase in Aspergillus oryzae. Eur J Biochem 88:113–120

    CAS  Google Scholar 

  • Tsushima H, Mine H, Kawakami Y, Hyodoh F, Ueki A (1994) Candida albicans aspartic proteinase cleaves and inactivates human epidermal cysteine proteinase inhibitor, cystatin A. Microbiology 140:167–171

    Article  PubMed  CAS  Google Scholar 

  • Van den Hazel HB, Killeand-Brandt MC, Winther JR (1993) The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region. J Biol Chem 268:18002–18007

    PubMed  Google Scholar 

  • Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D (1984) Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. J Bacteriol 159:811–819

    PubMed  CAS  Google Scholar 

  • Verheij H, Dijkstra BW (1994) Phospholipase A2: mechanism and structure. In: Woolley P, Petersen SV (eds) Lipases, their structure, biochemistry and application. Cambridge University Press, Cambridge, pp 119–138

    Google Scholar 

  • Von Heijne G (1986) A new method for predicting signal sequence cleavage sites. Nucl Acids Res 14:4683–4690

    Article  Google Scholar 

  • Wagner T, Borg von Zepelin M, Rüchel R (1995) pH-dependent denaturation of extracellular aspartic proteinases from Candida species. J Med Vet Mycol 33: 275–278

    Article  PubMed  CAS  Google Scholar 

  • Wain WH, Price MF, Cawson RA (1976) Factors affecting plaque formation by Candida albicans infecting the chick chorio-allantoic membrane. Sabouraudia 14:149–154

    Article  PubMed  CAS  Google Scholar 

  • Waldorf AR (1991) Cell-mediated host response to fungal aggression. In: Cole GT, Hoch HC (eds) The fungal spore and disease initiation in plants and animals. Plenum Press, New York, pp 445–460

    Google Scholar 

  • Warren NG, Shadomy HJ (1991) Yeasts of medical importance. In: Hansler WJ, Hermann KL, Isenberg HD, Shadomy HJ (eds) Manual of clinical microbiology, 5th edn. American Society for Microbiology Press, Washington, DC, pp 617–629

    Google Scholar 

  • Weatherburn MW (1967) Phenolhypochlorite reaction for determination of ammonia. Anal Chem 39:971–973

    Article  CAS  Google Scholar 

  • Weavers MD, Danuta JH, Gadek JE (1988) Alveolar fluid neutrophil elastase activity in the adult respiratory distress syndrome is complexed by alpha-2-macroglobulin. J Clin Invest 82:1260–1267

    Article  Google Scholar 

  • White T, Miyasaki SH, Agabian N (1993) Three distinct secreted aspartyl proteinases in Candida albicans. J Bacteriol 175:6126–6133

    PubMed  CAS  Google Scholar 

  • Winkler HH, Daugherty RM (1989) Phospholipase A activity associated with the growth of Rickettsia prowazekii in L929 cells. Infect Immun 57:36–40

    PubMed  CAS  Google Scholar 

  • Wolz C, Hellstern E, Haug M, Gallow DR, Vasil ML, Döring G (1991) Pseudomonas aeruginosa Las B mutant constructed by insertional mutagenesis reveals elastolytic activity due to alkaline proteinases and the Las A fragment. Mol Microbiol 5:2125–2131

    Article  PubMed  CAS  Google Scholar 

  • Wright RJ, Carne A, Hieber AD, Lamont IL, Emerson GW, Sullivan PA (1992) A second gene for a secreted aspartate proteinase in Candida albicans. J Bacteriol 174:7848–7853

    PubMed  CAS  Google Scholar 

  • Yu J, Yu DW, Checkla DM, Freedberg IM, Bertolino AP (1993) Human hair keratins. J Invest Dermatol 101: 56S–59S

    Article  Google Scholar 

  • Zubay G (1988) Biochemistry. Macmillan, New York

    Google Scholar 

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  1. Department of Microbiology, Medical College of Ohio, 3000 Arlington Avenue, P.O. 10008, Toledo, OH, 43699, USA

    G. T. Cole

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  1. Department of Microbiology and Immunology - 43-239 CHS, UCLA School of Medicine, Los Angeles, CA, 90024, USA

    Dexter H. Howard

  2. Plant Research Center, Mycotoxin Programme, Agriculture Canada, Ottawa, Ontario, K1A 0C6, Canada

    J. David Miller

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Cole, G.T. (1996). Biochemistry of Enzymatic Pathogenicity Factors. In: Howard, D.H., Miller, J.D. (eds) Human and Animal Relationships. The Mycota, vol 6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-10373-9_2

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