Biomaterial Database

Aspartic proteinases of Candida spp.: role in pathogenicity and antifungal resistance. 2014

Naiara C Silva, and Jéssica M Nery, and Amanda L T Dias

Microbiology and Immunology Department, Federal University of Alfenas (UNIFAL-MG), Alfenas, Minas Gerais, Brazil.

Fungal infections represent a serious health risk as they are particularly prevalent in immunocompromised individuals. Candida spp. pathogenicity depends on several factors and secreted aspartic proteinases (Sap) are considered one of the most critical factors as they are associated with adhesion, invasion and tissue damage. The production of proteinases is encoded by a family of 10 genes known as SAP, which are distributed differently among the species. The expression of these genes may be influenced by environmental conditions, which generally result in a higher fungal invasive potential. Non-pathogenic Candida spp. usually have fewer SAP genes, which are not necessarily expressed in the genome. Exposure to subinhibitory concentrations of antifungal agents promotes the development of resistant strains with an increased expression of SAP genes. In general, Candida spp. isolates that are resistant to antifungals show a higher secretion of Sap than the susceptible isolates. The relationship between Sap secretion and the susceptibility profile of the isolates is of great interest, although the role of SAPs in the development of resistance to antifungal agents remains still unclear. This review is the first one to address these issues.

UI	MeSH Term	Description	Entries
D009181	Mycoses	Diseases caused by FUNGI.	Fungus Diseases,Fungal Diseases,Fungal Infections,Fungus Infections,Disease, Fungal,Disease, Fungus,Diseases, Fungal,Diseases, Fungus,Fungal Disease,Fungal Infection,Fungus Disease,Fungus Infection,Infection, Fungal,Infection, Fungus,Infections, Fungal,Infections, Fungus
D002175	Candida	A genus of yeast-like mitosporic Saccharomycetales fungi characterized by producing yeast cells, mycelia, pseudomycelia, and blastophores. It is commonly part of the normal flora of the skin, mouth, intestinal tract, and vagina, but can cause a variety of infections, including CANDIDIASIS; ONYCHOMYCOSIS; VULVOVAGINAL CANDIDIASIS; and CANDIDIASIS, ORAL (THRUSH).	Candida guilliermondii var. nitratophila,Candida utilis,Cyberlindnera jadinii,Hansenula jadinii,Lindnera jadinii,Monilia,Pichia jadinii,Saccharomyces jadinii,Torula utilis,Torulopsis utilis,Monilias
D005656	Fungal Proteins	Proteins found in any species of fungus.	Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D000935	Antifungal Agents	Substances that destroy fungi by suppressing their ability to grow or reproduce. They differ from FUNGICIDES, INDUSTRIAL because they defend against fungi present in human or animal tissues.	Anti-Fungal Agents,Antifungal Agent,Fungicides, Therapeutic,Antibiotics, Antifungal,Therapeutic Fungicides,Agent, Antifungal,Anti Fungal Agents,Antifungal Antibiotics
D014774	Virulence	The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. The pathogenic capacity of an organism is determined by its VIRULENCE FACTORS.	Pathogenicity
D057055	Aspartic Acid Proteases	A subclass of peptide hydrolases that depend on an ASPARTIC ACID residue for their activity.	Aspartic Acid Protease,Aspartic Acid Proteinase,Aspartic Acid Proteinases,Aspartic Proteinase,Aspartic Proteinases,Aspartyl Protease,Aspartyl Proteinase,Aspartyl Proteinases,Aspartyl Proteases,Acid Protease, Aspartic,Acid Proteases, Aspartic,Acid Proteinase, Aspartic,Protease, Aspartic Acid,Protease, Aspartyl,Proteases, Aspartic Acid,Proteases, Aspartyl,Proteinase, Aspartic,Proteinase, Aspartic Acid,Proteinase, Aspartyl,Proteinases, Aspartic,Proteinases, Aspartic Acid,Proteinases, Aspartyl
D025141	Drug Resistance, Fungal	The ability of fungi to resist or to become tolerant to chemotherapeutic agents, antifungal agents, or antibiotics. This resistance may be acquired through gene mutation.	Antibiotic Resistance, Fungal,Antifungal Drug Resistance,Resistance, Antifungal Drug