Sequence of the<i>Candida albicans</i>gene encoding the secretory aspartate proteinase

Hube, Bernhard; Turver, C.J.; Odds, Frank C.; Eiffert, Helmut; Boulnois, Graham J.; Köchel, Heinrich G.; Rüchel, R.

doi:10.1080/02681219180000221

Cited by 111 publications

(73 citation statements)

References 10 publications

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“…A 23 amino acid sequence from N-terminus of C. albicans No. 114 proteinase indicated 70% homology to the enzyme cloned by Hube et al (1).…”

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confidence: 99%

“…Recently the gene encoding the secretory aspartate proteinase was cloned from a C. albicans ATCC 10231 genomic bank . The base sequence showed a 1,173 by open reading frame and a putative signal peptide consisting of 50 amino acid upstream of the active enzyme (1).…”

mentioning

confidence: 99%

“…N-terminal sequence of the proteinase from C. albicans No. 114 has 70% homology to the comparable enzyme cloned by Hube et al (1), but has no homology to C. albicans vacuolar aspartyl proteinase (4). Determination of the whole sequence from cDNA of C. albicans No.…”

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confidence: 99%

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Purification and Characterization of Secretory Proteinase of Candida albicans

Yamamoto

Nohara

Uchida

et al. 1992

Microbiology and Immunology

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Proteolytic activity of medically important yeasts was tested in both YCB-BSA agar and medium.All of 134 strains of Candida albicans, 13 of 18 strains of Candida tropicalis and 11 of 18 strains of Candida parapsilosis had this activity, while none of 52 Candida glabrata strains or of 11 Cryptococcus neoformans strains tested had proteolytic activity.Strains of C. albicans fell into five groups based on the level and time-course of in vitro proteinase productivity.Five strains randomly selected from each group were tested for pathogenicity in mice. The strain possessing the strongest pathogenicity was used to purify proteinase. The molecular weight of the proteinase was approximately 44,000 daltons and its isoelectric point was pH 4.2. Optimal pH of the proteinase was 3.2 and the enzyme was stable below pH 7.0 and lost its activity above pH 8.0 at 37 C in a 60-min incubation.The 23 amino acid sequence of the proteinase N-terminus was determined.

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“…A 23 amino acid sequence from N-terminus of C. albicans No. 114 proteinase indicated 70% homology to the enzyme cloned by Hube et al (1).…”

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confidence: 99%

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confidence: 99%

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Purification and Characterization of Secretory Proteinase of Candida albicans

Yamamoto

Nohara

Uchida

et al. 1992

Microbiology and Immunology

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“…The amino acid sequences of these aspartic proteinases were deduced from the corresponding genomic DNA sequences [ 1, 9 [5]), these proteinases offer a new target for the synthetic inhibitor design.…”

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confidence: 99%

Candida parapsilosis expresses and secretes two aspartic proteinases

et al. 1993

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We have Isolated and characterized a second aspartic proteinase secreted by the CHUV E-18 strain of Currt.Qda pcrrcrps~losts. This proteinase IS produced at a level correspondmg to approaimately 25% of the productlon of the mam protemase described earlier [l]. This minor protemase has similar molecular weight and pH optimum but differs m the lsoelectrlc point and m the specificity when compared with the major secreted form. The determmation of the ammo terminal amino acid sequence ldentlfied this mmor form of Citnriidti p~r~zp.~z~o.\/.~ aspartlc proteinase as a protein winch corresponds to the sequence deduced from genomlc DNA orlgmally reported as a pseudogene [l]. We conclude that strzun CHUV E-18 of Cu&idrr pmzps~/o.su expresses and secretes two different aspartlc proteinases.

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“…Two active aspartic acid sites, Asp-32 and Asp-218, and the amino acids near those sites were conserved in the C.albicans aspartic proteinase. Hube et al very recently reported the DNA sequence of secretory aspartate proteinase of another C. albicans strain, ATCC10231 (6). We compared their sequence with our cloned sequence, and found 76.9% DNA sequence homology and 61.6% amino acid homology (Fig.…”

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cDNA Cloning of an Aspartic Proteinase Secreted by Candida albicans

Mukai

Takeda

Asada

et al. 1992

Microbiology and Immunology

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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.Candida albicans is a major infectious fungal agent in humans, invading by attachment to the host cells via cell-surface adhesive molecules. Once attached, C.albicans cells proliferate and release extracellular aspartic proteinase, which aids them to invade the integument of the host. There seems to be a relationship between the production of aspartic proteinase by C. albicans and its virulence (7,9,14), but the actual role of the proteinase as the virulence factor remains unclear. Yamamoto et al (20) reported that all strains of C. albicans tested secrete the proteinase extracellularly, and they sequenced the first 23 amino acids of the N-terminal of the proteinase from their strain C. albicans No. 114. To understand its precise role, we have undertaken the cDNA cloning of this enzyme using PCR (polymerase chain reaction) with mixed primers constructed from the information published by that group.C. albicans serotype A, No. 114 and other Candida strains were obtained from

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Sequence of theCandida albicansgene encoding the secretory aspartate proteinase

Cited by 111 publications

References 10 publications

Purification and Characterization of Secretory Proteinase of Candida albicans

Purification and Characterization of Secretory Proteinase of Candida albicans

Candida parapsilosis expresses and secretes two aspartic proteinases

cDNA Cloning of an Aspartic Proteinase Secreted by Candida albicans

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