| Septins enforce morphogenetic events during sexual reproduction and contribute to virulence of Cryptococcus neoformans. | |
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MedLine Citation:
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PMID: 19943902 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Septins are conserved, cytoskeletal GTPases that contribute to cytokinesis, exocytosis, cell surface organization and vesicle fusion by mechanisms that are poorly understood. Roles of septins in morphogenesis and virulence of a human pathogen and basidiomycetous yeast Cryptococcus neoformans were investigated. In contrast to a well-established paradigm in S. cerevisiae, Cdc3 and Cdc12 septin homologues are dispensable for growth in C. neoformans yeast cells at 24 degrees C but are essential at 37 degrees C. In a bilateral cross between septin mutants, cells fuse but the resulting hyphae exhibit morphological abnormalities, including lack of properly fused specialized clamp cells and failure to produce spores. Interestingly, post-mating hyphae of the septin mutants have a defect in nuclear distribution. Thus, septins are essential for the development of spores, clamp cell fusion and also play a specific role in nuclear dynamics in hyphae. In the post-mating hyphae the septins localize to discrete sites in clamp connections, to the septa and the bases of the initial emerging spores. Strains lacking CDC3 or CDC12 exhibit significantly reduced virulence in a Galleria mellonella model of infection. Thus, C. neoformans septins are vital to morphology of the hyphae and contribute to virulence. |
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Authors:
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Lukasz Kozubowski; Joseph Heitman |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2009-11-25 |
Journal Detail:
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Title: Molecular microbiology Volume: 75 ISSN: 1365-2958 ISO Abbreviation: Mol. Microbiol. Publication Date: 2010 Feb |
Date Detail:
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Created Date: 2010-05-06 Completed Date: 2010-07-27 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8712028 Medline TA: Mol Microbiol Country: England |
Other Details:
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Languages: eng Pagination: 658-75 Citation Subset: IM |
Affiliation:
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Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cryptococcus neoformans
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cytology*,
pathogenicity*,
ultrastructure Cytoskeletal Proteins / analysis, classification, physiology* Fungal Proteins / analysis, classification, physiology* GTP Phosphohydrolases / analysis, classification, physiology* Humans Hyphae / chemistry, cytology, growth & development Morphogenesis Saccharomyces cerevisiae Proteins / classification Virulence |
| Grant Support | |
ID/Acronym/Agency:
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R01 AI39115/AI/NIAID NIH HHS; R01 AI42159/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cytoskeletal Proteins; 0/Fungal Proteins; 0/Saccharomyces cerevisiae Proteins; EC 3.6.1.-/GTP Phosphohydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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