Lipolytic Enzymes Involved in the Virulence of Human Pathogenic Fungi
DC Field | Value | Language |
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dc.contributor.author | Park, Minji | - |
dc.contributor.author | Do, Eunsoo | - |
dc.contributor.author | Jung, Won Hee | - |
dc.date.available | 2019-03-09T01:57:37Z | - |
dc.date.issued | 2013-06 | - |
dc.identifier.issn | 1229-8093 | - |
dc.identifier.issn | 2092-9323 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14631 | - |
dc.description.abstract | Pathogenic microbes secrete various enzymes with lipolytic activities to facilitate their survival within the host. Lipolytic enzymes include extracellular lipases and phospholipases, and several lines of evidence have suggested that these enzymes contribute to the virulence of pathogenic fungi. Candida albicans and Cryptococcus neoformans are the most commonly isolated human fungal pathogens, and several biochemical and molecular approaches have identified their extracellular lipolytic enzymes. The role of lipases and phospholipases in the virulence of C. albicans has been extensively studied, and these enzymes have been shown to contribute to C. albicans morphological transition, colonization, cytotoxicity, and penetration to the host. While not much is known about the lipases in C. neoformans, the roles of phospholipases in the dissemination of fungal cells in the host and in signaling pathways have been described. Lipolytic enzymes may also influence the survival of the lipophilic cutaneous pathogenic yeast Malassezia species within the host, and an unusually high number of lipase-coding genes may complement the lipid dependency of this fungus. This review briefly describes the current understanding of the lipolytic enzymes in major human fungal pathogens, namely C. albicans, C. neoformans, and Malassezia spp. | - |
dc.format.extent | 6 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | KOREAN SOC MYCOLOGY | - |
dc.title | Lipolytic Enzymes Involved in the Virulence of Human Pathogenic Fungi | - |
dc.type | Article | - |
dc.identifier.doi | 10.5941/MYCO.2013.41.2.67 | - |
dc.identifier.bibliographicCitation | MYCOBIOLOGY, v.41, no.2, pp 67 - 72 | - |
dc.identifier.kciid | ART001780420 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000326495100001 | - |
dc.identifier.scopusid | 2-s2.0-84885364129 | - |
dc.citation.endPage | 72 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 67 | - |
dc.citation.title | MYCOBIOLOGY | - |
dc.citation.volume | 41 | - |
dc.type.docType | Review | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Candida albicans | - |
dc.subject.keywordAuthor | Cryptococcus neoformans | - |
dc.subject.keywordAuthor | Lipase | - |
dc.subject.keywordAuthor | Lipolytic enzyme | - |
dc.subject.keywordAuthor | Malassezia | - |
dc.subject.keywordAuthor | Phospholipase | - |
dc.subject.keywordPlus | PHOSPHOLIPASE-D ACTIVITY | - |
dc.subject.keywordPlus | EXTRACELLULAR ENZYMATIC-ACTIVITY | - |
dc.subject.keywordPlus | CANDIDA-ALBICANS | - |
dc.subject.keywordPlus | CRYPTOCOCCUS-NEOFORMANS | - |
dc.subject.keywordPlus | MALASSEZIA-GLOBOSA | - |
dc.subject.keywordPlus | MOLECULAR-CLONING | - |
dc.subject.keywordPlus | LIPASE GENE | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | DIACYLGLYCEROL LIPASE | - |
dc.subject.keywordPlus | EXPRESSION ANALYSIS | - |
dc.relation.journalResearchArea | Agriculture | - |
dc.relation.journalResearchArea | Mycology | - |
dc.relation.journalWebOfScienceCategory | Agronomy | - |
dc.relation.journalWebOfScienceCategory | Mycology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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