COMPARATIVE STUDY ON HYDROLYTIC ENZYMES PRODUCED BY DIFFERENT MORPHOLOGICAL FORMS OF CANDIDA ALBICANS
Keywords:
Candida albicans, Candidiasis, Hydrolytic enzymes, Haemolytic activity, VirulenceAbstract
In recent years, the incidence of fungal infections has been rising all over the world. The ability of Candida albicans to switch from yeast to hyphal growth is essential for its virulence. The aim of this comparative study was to biotype and characterize phospholipase, proteinase, phosphatase and haemolytic activities of yeast and hyphal forms of Candida albicans. The hyphal form of Candida albicans secrets high quantity of hydrolytic enzymes than yeast form, which helps in its virulence. These results suggest that pathogenic fungi produce larger amount of inducible hydrolytic enzymes than non-pathogenic fungi. In this investigation, plate methods were used to determine the phospholipase, proteinase and haemolytic activities and spectrophotometric method was employed for testing acid phosphatase activity.
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Akcaglar S, Ener B, Tore O. Acid proteinase enzyme activity in Candida albicans strains: a comparison of spectrophotometry and plate methods. Tur J Biol 2010;35(2011):559-67.
Banno Y, Yamada T, Nozawa Y. Secreted phospholipases of the dimorphic fungus Candida albicans, separation of three enzymes and some biological properties. Sabouraudia 1985;23:47-54.
Barnett JA. A history of research on yeasts 12: medical yeasts part I, Candida albicans. Yeast 2008;25:385-417.
Bialkova A, Subik J. Biology of pathogenic yeast Candida glabrata. Folia Microbiol 2006;51:3-20.
Biswas SK, Yokoyama K, Nishimura K, Miyaji M. Effect of pH, Carbon source and K+ on the Na+-inhibited germ tube formation of Candida albicans. ISHAM Med Mycol 2000;38:363-9.
Borg M, Ruchel R. Expression of extracellular acid proteinase by proteolytic Candida spp. during experimental infection of oral mucosa. Infect Immun 1998;56:626-31.
Borges-Walmsley M, Walmsley AR. cAMP signaling in pathogenic fungi: control of dimorphic switching and pathogenicity. Trends Microbiol 2000;8:133-41.
Borman AM, Linton ChJ, Miles S J, Johnson EM. Molecular identification of pathogenic fungi. J Antimicrob Chemother 2008;61:i7-i12.
Bramono K, Tsuboi R, Murai M, Miyakawa Y, Fukazawa Y, Ogawa H. Scanning electron microscope observation of adherence of Candida albicans to cultured keratinocytes. J Med Vet Mycol 1994;32:473-6.
Bramono K, Yamazaki M, Tsuboi R, Hideoki O. Comparision of Proteinase, Lipase and Alpha Glucosidase activities from the clinical isolates of Candida Species. Jpn J Infect Dis 2006;59(2):73-6.
De Bernardis F, Arancia S, Morelli L, Hube B, Sanglard D, Schafer W, et al. Evidance that members of the secreted aspartyl proteinase gene family, in particular SAP2, are virulence factors for Candida vaginitis. J Infect Dis 1999;179:201-8.
Fradin C, Hube B. Tissue infection and site specific gene expression in Candida albicans. Adv Appl Microbiol 2003;53:271-90.
Ghosh S, Dhammika H, MLP Navarathna, Roberts DD, Copper JT, Atkin AL, et al. Arginine induced germ tube formation in Candida albicans is essential for escape from murine macrophage line RAW2/64.7 Infection Immunity 2009;77(4):1596-1605.
Ghosh S, Dhammika H, MLP Navarathna, Roberts DD, Copper JT, Atkin AL, et al. Arginine induced germ tube formation in Candida albicans is essential for escape from murine macrophage line RAW2/64.7 Infection Immunity 2009;77(4):1596-1605.
Gropper K, Schild L, Schindler S, Hube B, Zipfel PF, Skerka C. The yeast Candida albicans evades human complement attack by secretion of aspartic proteases. Mol Immun 2009;47:465-75.
Hube B, Sanglrd D, Odds FC, Hess D, Monod M, Schafer W, et al. Disruption of each of the secreted aspartyl proteinase genes SAP1, SAP2 and SAP3 of Candida albicans attenuates virulence. Infect Immum 1997;65:3529-38.
Lanzeta PA, Alvarez LJ, Reinach PS, Candia OA. An improved assay for nanomole amounts of inorganic phosphates. Anal Biochem 1979;100:95-7.
Leidich SD, Ibrahim AS, Fu Y. Cloning and disruption of caPLB1, a phospholipase B gene involved in the pathogenicity of Candida albicans. J Biol Chem 1998;273:26078-86.
Luo G, Samaranayake LP, Yau JYY. Candida species exhibit differential in vitro hemolytic activities. J Clin Microbiol 2001;39:2971-4.
Mahmoudabadi AZ, Zarrin M, Miry S. Phospholipase activity of candida albicans isolated from vagina & urine samples. Jundishapur J Microbiol 2010;3(4):169-73.
Manns JM, Mosser DM, Buckley HR. Production of hemolytic factor by Candida albicans. Infect Immun 1994;62:5154-6.
Mohandas V. Distribution of Candida species in different clinical samples and their virulence: biofilm formation, proteinase and phospholipase production: a study on hospitalized patients in southern Lindia. J Glob Infect Dis 2011;3:4-8.
Naglik J, Alberecht A, Bader O, Hube B. Candida albicans proteinases and host pathogen interactions. Cell Microbiol 2004;6:915-26.
Negi M, Tsuboi R, Matsui T, Ogawa H. Isolation and characterization of proteinase from Candida albicans: substrate specificity. J Invest Dermatol 1984;83:32-6.
Odds FC. Candida and Candidiasis: a review and bibliography. London: Bailliere Tindall; 1998.
Ogawa H, Tsuboi R. Fungal enzymes related to the pathogenesis of mycoses: In PH Jacob, L Nall (ed). Fungal disease. Marcel Dekker Inc, New York; 1997. p. 191-207.
Pei-Wen Tasi, Yu-Ting Chen, Po-Chen Hsu, Chung-Yu Lan. Study of Candida albicans and its interaction with the host: a mini review. Sci Direct (Elsevier) 2013;3:57-64.
Price MF, Wilkinson ID, Gentry LO. Plate method for detection of phospholipase activity in Candida albicans. Sabouraudia 1982;20:7-14.
Sachin CD, Ruchi k, Santosh S. In vitro evaluation of proteinase, phospholipase and haemolysin activities of Candida species isolated from clinical specimens. Int J Med Biomed Res 2012;1(2):153-7.
Samaranayake YH, Dassanayake RS, Cheung BPK, Jayatilake JA, Yeung KWS, Yauj YY, et al. Differential phospholipase gene expression by Candida albicans in artificial media and cultured human oral epithelium. APMIS 2006;114:857-66.
Sanglard D, Hube B, Monod M, Odds FC, Gow NA. A triple deletion of the secreted aspartyl proteinases genes SAP4, SAP5 and SAP6 of Candida albicans causes attenuated virulence. Infect Immun 1997;65:3539-46.
Silva S, Negri M, Henriques M, Oliveira R, Williams D, Azeredo J. Silicone colonization by non-Candida albicans Candida species in the presence of urine. J Med Mycol 2010;59:747-52.
Staniszewska M, Bondaryk M, Siennicka K, Pilat J, Schaller M, Kurzatkowski W. Role of Asparatic proteinases in Candida albicans virulence part. Int J Microbiol 2012;51(2):127-35.
Tsang CSP, Chu FCS, Leung WK, Jin LJ, Samaranayake LP, Siu SC. Phospholipase, Proteinase and Hemolytic activities of Candida albicans isolated from oral cavities of patients with type 2 diabetes mellitus. J Med Microbiol 2007;56:1393-8.
Tsuboi R, Kurita Y, Negi M, Ogawa H. A specific inhibitor of keratinolytic proteinases from Candida albicans could inhibit the cell growth of Candida albicans. J Invest Dermatol 1985;85:438-40.
Vasileva–Tonkova E, Galabova DN, Balasheva MA, Sotirova AV. Purification and partial characterization of acid phoshatase from Candida lipolytica. 1993;139:479-83.
Watts HJ, Cheah FS, Hube B, Sanglard D, Gow NA. Altered adherence in strains of Candida albicans harbouring null mutations in secreted aspartic proteinase genes. FEMS Microbiol let 1998;159:129-35.
Weinberg ED. Iron and infection. Microbiol Rev 1978;42:45-66.