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A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence
Hans-Knöll-Institute for Natural Products Research, Department of Infection Biology 1 and Department of Drug Testing 2 , Beutenbergstrasse 11, D-07745 Jena, Germany Friedrich Schiller University, Medical Faculty, Department of Molecular Cell Biology, Drackendorfer Strasse 1, D-07747 Jena, Germany 3...
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| Published in: | Microbiology (Society for General Microbiology) 2000-11, Vol.146 (11), p.2755-2764 |
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| container_end_page | 2764 |
| container_issue | 11 |
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| container_title | Microbiology (Society for General Microbiology) |
| container_volume | 146 |
| creator | Bruckmann, Astrid Kunkel, Waldemar Hartl, Albert Wetzker, Reinhard Eck, Raimund |
| description | Hans-Knöll-Institute for Natural Products Research, Department of Infection Biology 1 and Department of Drug Testing 2 , Beutenbergstrasse 11, D-07745 Jena, Germany
Friedrich Schiller University, Medical Faculty, Department of Molecular Cell Biology, Drackendorfer Strasse 1, D-07747 Jena, Germany 3
Author for correspondence: Raimund Eck. Tel: +49 3641 656852. Fax: +49 3641 656652. e-mail: reck{at}pmail.hki-jena.de
To determine if cellular functions of the phosphatidylinositol 3-kinase CaVps34p are related to processes governing Candida albicans pathogenicity, both copies of the gene were sequentially disrupted. Homozygous deletion of C. albicans VPS34 resulted in a mutant strain which exhibited defects not only in intracellular vesicle transport processes but also in morphogenesis. The CaVPS34 null mutant was unable to form hyphae on different solid media whilst showing a significantly delayed yeast-to-hyphae transition in liquid media. In addition, the mutant was rendered hypersensitive to temperature and osmotic stresses and had a strongly decreased ability to adhere to mouse fibroblast cells compared to the wild-type strain SC5314. Finally, evidence was obtained that CaVPS34 is essential for pathogenicity of C. albicans as the CaVPS34 null mutant was shown to be avirulent in a mouse model of systemic infection. C. albicans pathogenicity was restored to a near wild-type degree upon reintroduction of CaVPS34 into the chromosome of the null mutant, demonstrating that the observed avirulence corresponded to the loss of CaVPS34 . Thus, the results suggest that CaVPS34 may serve as a potential target for antifungal drugs.
Keywords: phosphatidylinositol 3-kinase, Candida albicans , gene disruption, virulence factors, pathogenicity Abbreviations: FCS, foetal calf serum; PI, phosphatidylinositol |
| doi_str_mv | 10.1099/00221287-146-11-2755 |
| format | article |
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Friedrich Schiller University, Medical Faculty, Department of Molecular Cell Biology, Drackendorfer Strasse 1, D-07747 Jena, Germany 3
Author for correspondence: Raimund Eck. Tel: +49 3641 656852. Fax: +49 3641 656652. e-mail: reck{at}pmail.hki-jena.de
To determine if cellular functions of the phosphatidylinositol 3-kinase CaVps34p are related to processes governing Candida albicans pathogenicity, both copies of the gene were sequentially disrupted. Homozygous deletion of C. albicans VPS34 resulted in a mutant strain which exhibited defects not only in intracellular vesicle transport processes but also in morphogenesis. The CaVPS34 null mutant was unable to form hyphae on different solid media whilst showing a significantly delayed yeast-to-hyphae transition in liquid media. In addition, the mutant was rendered hypersensitive to temperature and osmotic stresses and had a strongly decreased ability to adhere to mouse fibroblast cells compared to the wild-type strain SC5314. Finally, evidence was obtained that CaVPS34 is essential for pathogenicity of C. albicans as the CaVPS34 null mutant was shown to be avirulent in a mouse model of systemic infection. C. albicans pathogenicity was restored to a near wild-type degree upon reintroduction of CaVPS34 into the chromosome of the null mutant, demonstrating that the observed avirulence corresponded to the loss of CaVPS34 . Thus, the results suggest that CaVPS34 may serve as a potential target for antifungal drugs.
Keywords: phosphatidylinositol 3-kinase, Candida albicans , gene disruption, virulence factors, pathogenicity Abbreviations: FCS, foetal calf serum; PI, phosphatidylinositol</description><identifier>ISSN: 1350-0872</identifier><identifier>EISSN: 1465-2080</identifier><identifier>DOI: 10.1099/00221287-146-11-2755</identifier><identifier>PMID: 11065354</identifier><language>eng</language><publisher>Reading: Soc General Microbiol</publisher><subject>Animals ; Base Sequence ; Biological and medical sciences ; Candida albicans ; Candida albicans - enzymology ; Candida albicans - genetics ; Candida albicans - growth & development ; Candida albicans - pathogenicity ; Candidiasis - etiology ; CaVPS34 protein ; Cell Adhesion - physiology ; Cell Line ; DNA Primers - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Targeting ; Genes, Fungal ; Hot Temperature ; Humans ; Male ; Mice ; Microbiology ; Mycology ; Osmotic Pressure ; Pathogenicity, host-agent relations, miscellaneous strains, epidemiology ; Phosphatidylinositol 3-Kinases - genetics ; Phosphatidylinositol 3-Kinases - physiology ; Vacuoles - ultrastructure ; Virulence - genetics</subject><ispartof>Microbiology (Society for General Microbiology), 2000-11, Vol.146 (11), p.2755-2764</ispartof><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-fe7ff10412560645508d834a3accb9ae5f591a801605b3f624eb8d329ce1630b3</citedby><cites>FETCH-LOGICAL-c397t-fe7ff10412560645508d834a3accb9ae5f591a801605b3f624eb8d329ce1630b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=827031$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11065354$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bruckmann, Astrid</creatorcontrib><creatorcontrib>Kunkel, Waldemar</creatorcontrib><creatorcontrib>Hartl, Albert</creatorcontrib><creatorcontrib>Wetzker, Reinhard</creatorcontrib><creatorcontrib>Eck, Raimund</creatorcontrib><title>A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence</title><title>Microbiology (Society for General Microbiology)</title><addtitle>Microbiology</addtitle><description>Hans-Knöll-Institute for Natural Products Research, Department of Infection Biology 1 and Department of Drug Testing 2 , Beutenbergstrasse 11, D-07745 Jena, Germany
Friedrich Schiller University, Medical Faculty, Department of Molecular Cell Biology, Drackendorfer Strasse 1, D-07747 Jena, Germany 3
Author for correspondence: Raimund Eck. Tel: +49 3641 656852. Fax: +49 3641 656652. e-mail: reck{at}pmail.hki-jena.de
To determine if cellular functions of the phosphatidylinositol 3-kinase CaVps34p are related to processes governing Candida albicans pathogenicity, both copies of the gene were sequentially disrupted. Homozygous deletion of C. albicans VPS34 resulted in a mutant strain which exhibited defects not only in intracellular vesicle transport processes but also in morphogenesis. The CaVPS34 null mutant was unable to form hyphae on different solid media whilst showing a significantly delayed yeast-to-hyphae transition in liquid media. In addition, the mutant was rendered hypersensitive to temperature and osmotic stresses and had a strongly decreased ability to adhere to mouse fibroblast cells compared to the wild-type strain SC5314. Finally, evidence was obtained that CaVPS34 is essential for pathogenicity of C. albicans as the CaVPS34 null mutant was shown to be avirulent in a mouse model of systemic infection. C. albicans pathogenicity was restored to a near wild-type degree upon reintroduction of CaVPS34 into the chromosome of the null mutant, demonstrating that the observed avirulence corresponded to the loss of CaVPS34 . Thus, the results suggest that CaVPS34 may serve as a potential target for antifungal drugs.
Keywords: phosphatidylinositol 3-kinase, Candida albicans , gene disruption, virulence factors, pathogenicity Abbreviations: FCS, foetal calf serum; PI, phosphatidylinositol</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Candida albicans</subject><subject>Candida albicans - enzymology</subject><subject>Candida albicans - genetics</subject><subject>Candida albicans - growth & development</subject><subject>Candida albicans - pathogenicity</subject><subject>Candidiasis - etiology</subject><subject>CaVPS34 protein</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Line</subject><subject>DNA Primers - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Targeting</subject><subject>Genes, Fungal</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Male</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Mycology</subject><subject>Osmotic Pressure</subject><subject>Pathogenicity, host-agent relations, miscellaneous strains, epidemiology</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphatidylinositol 3-Kinases - physiology</subject><subject>Vacuoles - ultrastructure</subject><subject>Virulence - genetics</subject><issn>1350-0872</issn><issn>1465-2080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkU2LFDEQhhtR3HX1H4gEBA9itCrpdKePy-AXLHjRc0ink-loOhmT7l3235thxo-bp0qR5616qbdpniO8RRiGdwCMIZM9xbajiJT1QjxoLmsnKAMJD-ubC6Age3bRPCnlO0D9BHzcXCBCJ7hoLxt_TQ5zKodZr366Dz6m4tcUCKc_fNTFkuTITsfJT5roMHqjYyE-urDZaGwheppt8Sm-Ic4Hvdi4pq2QfU5360yqjtz6vIUj-7R55HQo9tm5XjXfPrz_uvtEb758_Ly7vqGGD_1Kne2dQ2iRiQ66VgiQk-St5tqYcdBWODGgloAdiJG7jrV2lBNng7HYcRj5VfPqNPeQ08_NllUtvhgbgo62elM940PLEf4LYi8FiKGvYHsCTU6lZOvUIftF53uFoI5ZqN9ZqHpghaiOWVTZi_P8bVzs9Fd0Pn4FXp4BXYwOLutofPnDSdYDx0q9PlGz3893Plu1t3Hx1cvoU7Vs_t35C9Csn84</recordid><startdate>20001101</startdate><enddate>20001101</enddate><creator>Bruckmann, Astrid</creator><creator>Kunkel, Waldemar</creator><creator>Hartl, Albert</creator><creator>Wetzker, Reinhard</creator><creator>Eck, Raimund</creator><general>Soc General Microbiol</general><general>Society for General Microbiology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20001101</creationdate><title>A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence</title><author>Bruckmann, Astrid ; Kunkel, Waldemar ; Hartl, Albert ; Wetzker, Reinhard ; Eck, Raimund</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-fe7ff10412560645508d834a3accb9ae5f591a801605b3f624eb8d329ce1630b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Candida albicans</topic><topic>Candida albicans - enzymology</topic><topic>Candida albicans - genetics</topic><topic>Candida albicans - growth & development</topic><topic>Candida albicans - pathogenicity</topic><topic>Candidiasis - etiology</topic><topic>CaVPS34 protein</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Line</topic><topic>DNA Primers - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Targeting</topic><topic>Genes, Fungal</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Male</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Mycology</topic><topic>Osmotic Pressure</topic><topic>Pathogenicity, host-agent relations, miscellaneous strains, epidemiology</topic><topic>Phosphatidylinositol 3-Kinases - genetics</topic><topic>Phosphatidylinositol 3-Kinases - physiology</topic><topic>Vacuoles - ultrastructure</topic><topic>Virulence - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bruckmann, Astrid</creatorcontrib><creatorcontrib>Kunkel, Waldemar</creatorcontrib><creatorcontrib>Hartl, Albert</creatorcontrib><creatorcontrib>Wetzker, Reinhard</creatorcontrib><creatorcontrib>Eck, Raimund</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Microbiology (Society for General Microbiology)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bruckmann, Astrid</au><au>Kunkel, Waldemar</au><au>Hartl, Albert</au><au>Wetzker, Reinhard</au><au>Eck, Raimund</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence</atitle><jtitle>Microbiology (Society for General Microbiology)</jtitle><addtitle>Microbiology</addtitle><date>2000-11-01</date><risdate>2000</risdate><volume>146</volume><issue>11</issue><spage>2755</spage><epage>2764</epage><pages>2755-2764</pages><issn>1350-0872</issn><eissn>1465-2080</eissn><abstract>Hans-Knöll-Institute for Natural Products Research, Department of Infection Biology 1 and Department of Drug Testing 2 , Beutenbergstrasse 11, D-07745 Jena, Germany
Friedrich Schiller University, Medical Faculty, Department of Molecular Cell Biology, Drackendorfer Strasse 1, D-07747 Jena, Germany 3
Author for correspondence: Raimund Eck. Tel: +49 3641 656852. Fax: +49 3641 656652. e-mail: reck{at}pmail.hki-jena.de
To determine if cellular functions of the phosphatidylinositol 3-kinase CaVps34p are related to processes governing Candida albicans pathogenicity, both copies of the gene were sequentially disrupted. Homozygous deletion of C. albicans VPS34 resulted in a mutant strain which exhibited defects not only in intracellular vesicle transport processes but also in morphogenesis. The CaVPS34 null mutant was unable to form hyphae on different solid media whilst showing a significantly delayed yeast-to-hyphae transition in liquid media. In addition, the mutant was rendered hypersensitive to temperature and osmotic stresses and had a strongly decreased ability to adhere to mouse fibroblast cells compared to the wild-type strain SC5314. Finally, evidence was obtained that CaVPS34 is essential for pathogenicity of C. albicans as the CaVPS34 null mutant was shown to be avirulent in a mouse model of systemic infection. C. albicans pathogenicity was restored to a near wild-type degree upon reintroduction of CaVPS34 into the chromosome of the null mutant, demonstrating that the observed avirulence corresponded to the loss of CaVPS34 . Thus, the results suggest that CaVPS34 may serve as a potential target for antifungal drugs.
Keywords: phosphatidylinositol 3-kinase, Candida albicans , gene disruption, virulence factors, pathogenicity Abbreviations: FCS, foetal calf serum; PI, phosphatidylinositol</abstract><cop>Reading</cop><pub>Soc General Microbiol</pub><pmid>11065354</pmid><doi>10.1099/00221287-146-11-2755</doi><tpages>10</tpages></addata></record> |
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| identifier | ISSN: 1350-0872 |
| ispartof | Microbiology (Society for General Microbiology), 2000-11, Vol.146 (11), p.2755-2764 |
| issn | 1350-0872 1465-2080 |
| language | eng |
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| source | Alma/SFX Local Collection |
| subjects | Animals Base Sequence Biological and medical sciences Candida albicans Candida albicans - enzymology Candida albicans - genetics Candida albicans - growth & development Candida albicans - pathogenicity Candidiasis - etiology CaVPS34 protein Cell Adhesion - physiology Cell Line DNA Primers - genetics Fundamental and applied biological sciences. Psychology Gene Targeting Genes, Fungal Hot Temperature Humans Male Mice Microbiology Mycology Osmotic Pressure Pathogenicity, host-agent relations, miscellaneous strains, epidemiology Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - physiology Vacuoles - ultrastructure Virulence - genetics |
| title | A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence |
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