DetoxFungiV1, Main, Exploration, bibRecord, 000F72

HapX Mediates Iron Homeostasis in the Pathogenic Dermatophyte Arthroderma benhamiae but Is Dispensable for Virulence.

Identifieur interne : 000F72 ( Main/Exploration ); précédent : 000F71; suivant : 000F73

HapX Mediates Iron Homeostasis in the Pathogenic Dermatophyte Arthroderma benhamiae but Is Dispensable for Virulence.

Auteurs : Antje Kröber [Allemagne] ; Kirstin Scherlach [Allemagne] ; Peter Hortschansky [Allemagne] ; Ekaterina Shelest [Allemagne] ; Peter Staib [Allemagne] ; Olaf Kniemeyer [Allemagne] ; Axel A. Brakhage [Allemagne]

Source :

PloS one [ 1932-6203 ] ; 2016.

RBID : pubmed:26960149

Descripteurs français

KwdFr :
- Arthrodermataceae (croissance et développement), Arthrodermataceae (génétique), Arthrodermataceae (pathogénicité), Fer (métabolisme), Fer (pharmacologie), Gènes fongiques (MeSH), Homéostasie (effets des médicaments et des substances chimiques), Homéostasie (génétique), Humains (MeSH), Hyphae (effets des médicaments et des substances chimiques), Hyphae (physiologie), Kératines (pharmacologie), Mutation (génétique), Pigmentation (effets des médicaments et des substances chimiques), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Sidérophores (métabolisme), Similitude de séquences d'acides aminés (MeSH), Spores fongiques (effets des médicaments et des substances chimiques), Spores fongiques (physiologie), Virulence (effets des médicaments et des substances chimiques), Virulence (génétique).
MESH :
- croissance et développement : Arthrodermataceae.
- effets des médicaments et des substances chimiques : Homéostasie, Hyphae, Pigmentation, Régulation de l'expression des gènes fongiques, Spores fongiques, Virulence.
- génétique : Arthrodermataceae, Homéostasie, Mutation, Protéines fongiques, Virulence.
- métabolisme : Fer, Protéines fongiques, Sidérophores.
- pathogénicité : Arthrodermataceae.
- pharmacologie : Fer, Kératines.
- physiologie : Hyphae, Spores fongiques.
- Gènes fongiques, Humains, Similitude de séquences d'acides aminés.

English descriptors

KwdEn :
- Arthrodermataceae (genetics), Arthrodermataceae (growth & development), Arthrodermataceae (pathogenicity), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (drug effects), Genes, Fungal (MeSH), Homeostasis (drug effects), Homeostasis (genetics), Humans (MeSH), Hyphae (drug effects), Hyphae (physiology), Iron (metabolism), Iron (pharmacology), Keratins (pharmacology), Mutation (genetics), Pigmentation (drug effects), Sequence Homology, Amino Acid (MeSH), Siderophores (metabolism), Spores, Fungal (drug effects), Spores, Fungal (physiology), Virulence (drug effects), Virulence (genetics).
MESH :
- chemical , genetics : Fungal Proteins.
- drug effects : Gene Expression Regulation, Fungal, Homeostasis, Hyphae, Pigmentation, Spores, Fungal, Virulence.
- genetics : Arthrodermataceae, Homeostasis, Mutation, Virulence.
- growth & development : Arthrodermataceae.
- chemical , metabolism : Fungal Proteins, Iron, Siderophores.
- pathogenicity : Arthrodermataceae.
- chemical , pharmacology : Iron, Keratins.
- physiology : Hyphae, Spores, Fungal.
- Genes, Fungal, Humans, Sequence Homology, Amino Acid.

Abstract

For many pathogenic fungi, siderophore-mediated iron acquisition is essential for virulence. The process of siderophore production and further mechanisms to adapt to iron limitation are strictly controlled in fungi to maintain iron homeostasis. Here we demonstrate that the human pathogenic dermatophyte Arthroderma benhamiae produces the hydroxamate siderophores ferricrocin and ferrichrome C. Additionally, we show that the iron regulator HapX is crucial for the adaptation to iron starvation and iron excess, but is dispensable for virulence of A. benhamiae. Deletion of hapX caused downregulation of siderophore biosynthesis genes leading to a decreased production of siderophores during iron starvation. Furthermore, HapX was required for transcriptional repression of genes involved in iron-dependent pathways during iron-depleted conditions. Additionally, the ΔhapX mutant of A. benhamiae was sensitive to high-iron concentrations indicating that HapX also contributes to iron detoxification. In contrast to other pathogenic fungi, HapX of A. benhamiae was redundant for virulence and a ΔhapX mutant was still able to infect keratinized host tissues in vitro. Our findings underline the highly conserved role of the transcription factor HapX for maintaining iron homeostasis in ascomycetous fungi but, unlike in many other human and plant pathogenic fungi, HapX of A. benhamiae is not a virulence determinant.

DOI: 10.1371/journal.pone.0150701
PubMed: 26960149
PubMed Central: PMC4784894

Affiliations:

Allemagne

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000F87
to stream Main, to step Curation: 000F87

Le document en format XML

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<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression Regulation, Fungal (drug effects)</term>
<term>Genes, Fungal (MeSH)</term>
<term>Homeostasis (drug effects)</term>
<term>Homeostasis (genetics)</term>
<term>Humans (MeSH)</term>
<term>Hyphae (drug effects)</term>
<term>Hyphae (physiology)</term>
<term>Iron (metabolism)</term>
<term>Iron (pharmacology)</term>
<term>Keratins (pharmacology)</term>
<term>Mutation (genetics)</term>
<term>Pigmentation (drug effects)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Siderophores (metabolism)</term>
<term>Spores, Fungal (drug effects)</term>
<term>Spores, Fungal (physiology)</term>
<term>Virulence (drug effects)</term>
<term>Virulence (genetics)</term>
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<term>Homéostasie (génétique)</term>
<term>Humains (MeSH)</term>
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<term>Hyphae (physiologie)</term>
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<term>Mutation (génétique)</term>
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<term>Protéines fongiques (métabolisme)</term>
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<term>Sidérophores (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
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<term>Régulation de l'expression des gènes fongiques</term>
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<term>Virulence</term>
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<term>Virulence</term>
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<term>Siderophores</term>
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<term>Protéines fongiques</term>
<term>Sidérophores</term>
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<term>Kératines</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Iron</term>
<term>Keratins</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Hyphae</term>
<term>Spores fongiques</term>
</keywords>
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</keywords>
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<term>Humans</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
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<term>Humains</term>
<term>Similitude de séquences d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">For many pathogenic fungi, siderophore-mediated iron acquisition is essential for virulence. The process of siderophore production and further mechanisms to adapt to iron limitation are strictly controlled in fungi to maintain iron homeostasis. Here we demonstrate that the human pathogenic dermatophyte Arthroderma benhamiae produces the hydroxamate siderophores ferricrocin and ferrichrome C. Additionally, we show that the iron regulator HapX is crucial for the adaptation to iron starvation and iron excess, but is dispensable for virulence of A. benhamiae. Deletion of hapX caused downregulation of siderophore biosynthesis genes leading to a decreased production of siderophores during iron starvation. Furthermore, HapX was required for transcriptional repression of genes involved in iron-dependent pathways during iron-depleted conditions. Additionally, the ΔhapX mutant of A. benhamiae was sensitive to high-iron concentrations indicating that HapX also contributes to iron detoxification. In contrast to other pathogenic fungi, HapX of A. benhamiae was redundant for virulence and a ΔhapX mutant was still able to infect keratinized host tissues in vitro. Our findings underline the highly conserved role of the transcription factor HapX for maintaining iron homeostasis in ascomycetous fungi but, unlike in many other human and plant pathogenic fungi, HapX of A. benhamiae is not a virulence determinant. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26960149</PMID>
<DateCompleted><Year>2016</Year>
<Month>07</Month>
<Day>25</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>02</Month>
<Day>19</Day>
</DateRevised>
<Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>11</Volume>
<Issue>3</Issue>
<PubDate><Year>2016</Year>
</PubDate>
</JournalIssue>
<Title>PloS one</Title>
<ISOAbbreviation>PLoS One</ISOAbbreviation>
</Journal>
<ArticleTitle>HapX Mediates Iron Homeostasis in the Pathogenic Dermatophyte Arthroderma benhamiae but Is Dispensable for Virulence.</ArticleTitle>
<Pagination><MedlinePgn>e0150701</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0150701</ELocationID>
<Abstract><AbstractText>For many pathogenic fungi, siderophore-mediated iron acquisition is essential for virulence. The process of siderophore production and further mechanisms to adapt to iron limitation are strictly controlled in fungi to maintain iron homeostasis. Here we demonstrate that the human pathogenic dermatophyte Arthroderma benhamiae produces the hydroxamate siderophores ferricrocin and ferrichrome C. Additionally, we show that the iron regulator HapX is crucial for the adaptation to iron starvation and iron excess, but is dispensable for virulence of A. benhamiae. Deletion of hapX caused downregulation of siderophore biosynthesis genes leading to a decreased production of siderophores during iron starvation. Furthermore, HapX was required for transcriptional repression of genes involved in iron-dependent pathways during iron-depleted conditions. Additionally, the ΔhapX mutant of A. benhamiae was sensitive to high-iron concentrations indicating that HapX also contributes to iron detoxification. In contrast to other pathogenic fungi, HapX of A. benhamiae was redundant for virulence and a ΔhapX mutant was still able to infect keratinized host tissues in vitro. Our findings underline the highly conserved role of the transcription factor HapX for maintaining iron homeostasis in ascomycetous fungi but, unlike in many other human and plant pathogenic fungi, HapX of A. benhamiae is not a virulence determinant. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kröber</LastName>
<ForeName>Antje</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Junior Research Group Fundamental Molecular Biology of Pathogenic Fungi, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Scherlach</LastName>
<ForeName>Kirstin</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hortschansky</LastName>
<ForeName>Peter</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shelest</LastName>
<ForeName>Ekaterina</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Systems Biology and Bioinformatics, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Staib</LastName>
<ForeName>Peter</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Junior Research Group Fundamental Molecular Biology of Pathogenic Fungi, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kniemeyer</LastName>
<ForeName>Olaf</ForeName>
<Initials>O</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Institute of Microbiology, Friedrich Schiller University, Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Brakhage</LastName>
<ForeName>Axel A</ForeName>
<Initials>AA</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Jena, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Institute of Microbiology, Friedrich Schiller University, Jena, Germany.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>03</Month>
<Day>09</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>PLoS One</MedlineTA>
<NlmUniqueID>101285081</NlmUniqueID>
<ISSNLinking>1932-6203</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017262">Siderophores</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>68238-35-7</RegistryNumber>
<NameOfSubstance UI="D007633">Keratins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>E1UOL152H7</RegistryNumber>
<NameOfSubstance UI="D007501">Iron</NameOfSubstance>
</Chemical>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D003883" MajorTopicYN="N">Arthrodermataceae</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006706" MajorTopicYN="Y">Homeostasis</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D025301" MajorTopicYN="N">Hyphae</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007633" MajorTopicYN="N">Keratins</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010858" MajorTopicYN="N">Pigmentation</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017262" MajorTopicYN="N">Siderophores</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013172" MajorTopicYN="N">Spores, Fungal</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014774" MajorTopicYN="N">Virulence</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<affiliations><list><country><li>Allemagne</li>
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<name sortKey="Hortschansky, Peter" sort="Hortschansky, Peter" uniqKey="Hortschansky P" first="Peter" last="Hortschansky">Peter Hortschansky</name>
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HapX Mediates Iron Homeostasis in the Pathogenic Dermatophyte Arthroderma benhamiae but Is Dispensable for Virulence.

HapX Mediates Iron Homeostasis in the Pathogenic Dermatophyte Arthroderma benhamiae but Is Dispensable for Virulence.

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