cDNA Cloning of an Aspartic Proteinase Secreted by Candida albicans

cDNA of an aspartic proteinase secreted by Candida albicans No. 114 was isolated using the polymerase chain reaction (PCR). The primary structure of the enzyme was deduced from the nucleotide sequence of the cDNA and compared with the structures of Saccharomyces cerevisiae proteinase A and vacuolar aspartyl proteinase of C. albicans. The mature aspartic proteinase consisted of 341 amino acid residues, and was 17.6 and 15.3% identical with the proteinase A and the aspartyl proteinase, respectively. Two active aspartic acid sites and the amino acids near those sites were conserved in the aspartic proteinase. We also showed that there is another gene of aspartic proteinase than that of strain ATCC10231 reported by Hube et al (J. Med. Vet. Mycol. 29 (1991)) in the same C. albicans genome, both in that strain and in No. 114.

[1]  Tetsurou Yamamoto,et al.  Purification and Characterization of Secretory Proteinase of Candida albicans , 1992, Microbiology and immunology.

[2]  A. Brown,et al.  Codon utilisation in the pathogenic yeast, Candida albicans. , 1991, Nucleic acids research.

[3]  R. Falchetto,et al.  Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis , 1991, FEBS letters.

[4]  T. Hikiji,et al.  Evidence that more than one gene encodes n-alkane-inducible cytochrome P-450s in Candida maltosa, found by two-step gene disruption. , 1991, Agricultural and biological chemistry.

[5]  G. Boulnois,et al.  Sequence of the Candida albicans gene encoding the secretory aspartate proteinase. , 1991, Journal of medical and veterinary mycology : bi-monthly publication of the International Society for Human and Animal Mycology.

[6]  T. Lott,et al.  Nucleotide sequence of the Candida albicans aspartyl proteinase gene. , 1989, Nucleic acids research.

[7]  T. Stevens,et al.  PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors , 1986, Molecular and cellular biology.

[8]  P. T. Magee,et al.  Genetic evidence for role of extracellular proteinase in virulence of Candida albicans , 1985, Infection and immunity.

[9]  J. Chirgwin,et al.  Cloning and sequence analysis of cDNA for human cathepsin D. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[10]  A. Fedorov,et al.  Structure of ethanol-inhibited porcine pepsin at 2-A resolution and binding of the methyl ester of phenylalanyl-diiodotyrosine to the enzyme. , 1984, The Journal of biological chemistry.

[11]  R. Rüchel On the role of proteinases from Candida albicans in the pathogenesis of acronecrosis. , 1983, Zentralblatt fur Bakteriologie, Mikrobiologie und Hygiene. 1. Abt. Originale A, Medizinische Mikrobiologie, Infektionskrankheiten und Parasitologie = International journal of microbiology and hygiene. A, Medical microbiology, infectious....

[12]  D Perlman,et al.  A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. , 1983, Journal of molecular biology.

[13]  F. Macdonald,et al.  Virulence for mice of a proteinase-secreting strain of Candida albicans and a proteinase-deficient mutant. , 1983, Journal of general microbiology.

[14]  M. Trost,et al.  A comparison of secretory proteinases from different strains of Candida albicans. , 1982, Sabouraudia.

[15]  R. Rüchel Properties of a purified proteinase from the yeast Candida albicans. , 1981, Biochimica et biophysica acta.

[16]  M. James,et al.  Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin , 1977, Nature.

[17]  T. Blundell,et al.  Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[18]  M. Losada,et al.  Interconversion of the active and inactive forms ofChlorella nitrate reductase , 1972, FEBS letters.

[19]  J. Warner,et al.  Isolation, characterization, and translation of mRNA from yeast. , 1978, Methods in cell biology.