study on the role of secreted aspartic proteinase (SAP2) of Candida Albicans in the pathogenesis of candidal infections.
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study on the role of secreted aspartic proteinase (SAP2) of Candida Albicans in the pathogenesis of candidal infections. by Ali Ghadjari

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Published by University of Manchester in Manchester .
Written in English


Book details:

Edition Notes

Thesis (Ph.D.) - University of Manchester, Faculty of Medicine.

ContributionsUniversity of Manchester. Faculty of Medicine.
The Physical Object
Pagination272p.
Number of Pages272
ID Numbers
Open LibraryOL17161211M

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Secreted aspartic proteinase (Sap) activity contributes to tissue damage in a model of human oral candidosis. In this study, The importance of Saps in establishing systemic and vaginal C. albicans infections was demonstrated by the protective role of the proteinase inhibitor, pepstatin A. Bacterial Aspartic Proteinases as Novel Antibiotic Targets p. Structural Thermodynamic Study of the Binding of Renin Inhibitors to Endothiapepsin p. Development and Testing of Inhibitors of Candida Aspartic Proteinases p. Primary Substrate Specificities of Secreted Aspartic Proteases of Candida albicans p. Functional Aspects of. The VIIth International Conference on Aspartic Proteinases was held in Banff, Alberta, Canada, from October 22 to 27, The venue was the Banff Centre in the Canadian Rockies, a setting well known worldwide for the scenic beauty and mountain grandeur. Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_, which encodes for a hypothetical protein, is the focus in this study. A recombinant enzyme Amuc_ containing the 6×; His-tag produced in Escherichia coli.

SUMMARY Candida albicans is the most common fungal pathogen of humans and has developed an extensive repertoire of putative virulence mechanisms that allows successful colonization and infection of the host under suitable predisposing conditions. Extracellular proteolytic activity plays a central role in Candida pathogenicity and is produced by a family of 10 secreted aspartyl proteinases (Sap. The lysosomal aspartic proteinase cathepsin D has been implicated in tumorigenesis and the stomach enzyme pepsin, which plays a major physiological role in hydrolysis of acid-denatured proteins, is responsible for much of the tissue damage in peptic ulcer disease. Aspartic Proteinase. Aspartic proteinases have reported to have a considerable role in the degradation of heterologous proteins produced in e.g. Aspergillus which has led to mutagenesis and screening for protease negative/low protease mutant strains (Mattern et al. ) and disruption of the gene encoding aspartic proteinase enzyme (Berka et al. ). Secreted aspartyl proteinases (Saps), encoded by a gene family with at least nine members (SAP1 to SAP9), are one of the most discussed virulence factors produced by the human pathogen Candida albicans. In order to study the role of each Sap isoenzyme in pathogenicity, we have constructed strains which harbor mutations at selected SAP genes.

  A novel aspartic proteinase (BmCatD) gene cloned from the silkworm B. mori. The BmCatD cDNA was isolated by searching B. mori ESTs that encode a protein of amino acids (GenBank accession number AY). Comparison of amplicon size between the genomic and cDNA sequences revealed the presence of nine exons and eight introns in BmCatD (Fig. 1A).The two catalytic centers and aspartic .   Abstract. Candida albicans—a common opportunistic fungal pathogen of humans—causes serious, disseminated invasive infections (candidiases) executed due to the action of several groups of virulence of the most critical is a family of secreted aspartic proteases involved in the destruction of host proteins and tissues. Secreted aspartyl proteinases (Saps) contribute to the ability of Candida albicans to cause mucosal and disseminated infections. A model of vaginal candidiasis based on reconstituted human vaginal epithelium (RHVE) was used to study the expression and role of these C. albicans proteinases during infection and tissue damage of vaginal epithelium. Colonization of the RHVE by C. albicans SC Akkermansia muciniphila can produce various mucin-degrading proteins. However, the functional characteristics of these proteins and their role in mucin degradation are unclear. Of the predicted protein-coding genes, Amuc_, which encodes for a hypothetical protein, is the focus in this study.A recombinant enzyme Amuc_ containing the 6× His-tag produced in Escherichia coli (hereinafter.