Rapamycin and less immunosuppressive analogs are toxic to Candida albicans and Cryptococcus neoformans via FKBP12-dependent inhibition of TOR.
Identifieur interne : 001A06 ( Main/Exploration ); précédent : 001A05; suivant : 001A07Rapamycin and less immunosuppressive analogs are toxic to Candida albicans and Cryptococcus neoformans via FKBP12-dependent inhibition of TOR.
Auteurs : M C Cruz [États-Unis] ; A L Goldstein ; J. Blankenship ; M. Del Poeta ; J R Perfect ; J H Mccusker ; Y L Bennani ; M E Cardenas ; J. HeitmanSource :
- Antimicrobial agents and chemotherapy [ 0066-4804 ] ; 2001.
Descripteurs français
- KwdFr :
- Amorces ADN (MeSH), Antifongiques (pharmacologie), Candida albicans (effets des médicaments et des substances chimiques), Candida albicans (génétique), Cryptococcus neoformans (croissance et développement), Cryptococcus neoformans (effets des médicaments et des substances chimiques), Immunosuppresseurs (pharmacologie), Milieux de culture (MeSH), Mutagenèse (MeSH), Phosphatidylinositol 3-kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (effets des médicaments et des substances chimiques), Phosphotransferases (Alcohol Group Acceptor) (génétique), Protéine 1A de liaison au tacrolimus (effets des médicaments et des substances chimiques), Protéines de Saccharomyces cerevisiae (MeSH), Protéines fongiques (effets des médicaments et des substances chimiques), Protéines fongiques (génétique), RT-PCR (MeSH), Recombinaison génétique (MeSH), Résistance aux substances (MeSH), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (génétique), Sirolimus (analogues et dérivés), Sirolimus (pharmacologie).
- MESH :
- analogues et dérivés : Sirolimus.
- croissance et développement : Cryptococcus neoformans, Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Candida albicans, Cryptococcus neoformans, Phosphotransferases (Alcohol Group Acceptor), Protéine 1A de liaison au tacrolimus, Protéines fongiques.
- génétique : Candida albicans, Phosphotransferases (Alcohol Group Acceptor), Protéines fongiques, Saccharomyces cerevisiae.
- pharmacologie : Antifongiques, Immunosuppresseurs, Sirolimus.
- Amorces ADN, Milieux de culture, Mutagenèse, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, RT-PCR, Recombinaison génétique, Résistance aux substances.
English descriptors
- KwdEn :
- Antifungal Agents (pharmacology), Candida albicans (drug effects), Candida albicans (genetics), Cryptococcus neoformans (drug effects), Cryptococcus neoformans (growth & development), Culture Media (MeSH), DNA Primers (MeSH), Drug Resistance (MeSH), Fungal Proteins (drug effects), Fungal Proteins (genetics), Immunosuppressive Agents (pharmacology), Mutagenesis (MeSH), Phosphatidylinositol 3-Kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (drug effects), Phosphotransferases (Alcohol Group Acceptor) (genetics), Recombination, Genetic (MeSH), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae Proteins (MeSH), Sirolimus (analogs & derivatives), Sirolimus (pharmacology), Tacrolimus Binding Protein 1A (drug effects).
- MESH :
- chemical , analogs & derivatives : Sirolimus.
- chemical , drug effects : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor), Tacrolimus Binding Protein 1A.
- chemical , genetics : Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor).
- chemical , pharmacology : Antifungal Agents, Immunosuppressive Agents, Sirolimus.
- drug effects : Candida albicans, Cryptococcus neoformans.
- genetics : Candida albicans, Saccharomyces cerevisiae.
- growth & development : Cryptococcus neoformans, Saccharomyces cerevisiae.
- chemical : Culture Media, DNA Primers, Drug Resistance, Mutagenesis, Phosphatidylinositol 3-Kinases, Recombination, Genetic, Reverse Transcriptase Polymerase Chain Reaction, Saccharomyces cerevisiae Proteins.
Abstract
Candida albicans and Cryptococcus neoformans cause both superficial and disseminated infections in humans. Current antifungal therapies for deep-seated infections are limited to amphotericin B, flucytosine, and azoles. A limitation is that commonly used azoles are fungistatic in vitro and in vivo. Our studies address the mechanisms of antifungal activity of the immunosuppressive drug rapamycin (sirolimus) and its analogs with decreased immunosuppressive activity. C. albicans rbp1/rbp1 mutant strains lacking a homolog of the FK506-rapamycin target protein FKBP12 were found to be viable and resistant to rapamycin and its analogs. Rapamycin and analogs promoted FKBP12 binding to the wild-type Tor1 kinase but not to a rapamycin-resistant Tor1 mutant kinase (S1972R). FKBP12 and TOR mutations conferred resistance to rapamycin and its analogs in C. albicans, C. neoformans, and Saccharomyces cerevisiae. Our findings demonstrate the antifungal activity of rapamycin and rapamycin analogs is mediated via conserved complexes with FKBP12 and Tor kinase homologs in divergent yeasts. Taken together with our observations that rapamycin and its analogs are fungicidal and that spontaneous drug resistance occurs at a low rate, these mechanistic findings support continued investigation of rapamycin analogs as novel antifungal agents.
DOI: 10.1128/AAC.45.11.3162-3170.2001
PubMed: 11600372
PubMed Central: PMC90798
Affiliations:
Links toward previous steps (curation, corpus...)
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Blankenship</name></author><author><name sortKey="Del Poeta, M" sort="Del Poeta, M" uniqKey="Del Poeta M" first="M" last="Del Poeta">M. Del Poeta</name></author><author><name sortKey="Perfect, J R" sort="Perfect, J R" uniqKey="Perfect J" first="J R" last="Perfect">J R Perfect</name></author><author><name sortKey="Mccusker, J H" sort="Mccusker, J H" uniqKey="Mccusker J" first="J H" last="Mccusker">J H Mccusker</name></author><author><name sortKey="Bennani, Y L" sort="Bennani, Y L" uniqKey="Bennani Y" first="Y L" last="Bennani">Y L Bennani</name></author><author><name sortKey="Cardenas, M E" sort="Cardenas, M E" uniqKey="Cardenas M" first="M E" last="Cardenas">M E Cardenas</name></author><author><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. Heitman</name></author></analytic><series><title level="j">Antimicrobial agents and chemotherapy</title><idno type="ISSN">0066-4804</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antifungal Agents (pharmacology)</term><term>Candida albicans (drug effects)</term><term>Candida albicans (genetics)</term><term>Cryptococcus neoformans (drug effects)</term><term>Cryptococcus neoformans (growth & development)</term><term>Culture Media (MeSH)</term><term>DNA Primers (MeSH)</term><term>Drug Resistance (MeSH)</term><term>Fungal Proteins (drug effects)</term><term>Fungal Proteins (genetics)</term><term>Immunosuppressive Agents (pharmacology)</term><term>Mutagenesis (MeSH)</term><term>Phosphatidylinositol 3-Kinases (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (drug effects)</term><term>Phosphotransferases (Alcohol Group Acceptor) (genetics)</term><term>Recombination, Genetic (MeSH)</term><term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Sirolimus (analogs & derivatives)</term><term>Sirolimus (pharmacology)</term><term>Tacrolimus Binding Protein 1A (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN (MeSH)</term><term>Antifongiques (pharmacologie)</term><term>Candida albicans (effets des médicaments et des substances chimiques)</term><term>Candida albicans (génétique)</term><term>Cryptococcus neoformans (croissance et développement)</term><term>Cryptococcus neoformans (effets des médicaments et des substances chimiques)</term><term>Immunosuppresseurs (pharmacologie)</term><term>Milieux de culture (MeSH)</term><term>Mutagenèse (MeSH)</term><term>Phosphatidylinositol 3-kinases (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (effets des médicaments et des substances chimiques)</term><term>Phosphotransferases (Alcohol Group Acceptor) (génétique)</term><term>Protéine 1A de liaison au tacrolimus (effets des médicaments et des substances chimiques)</term><term>Protéines de Saccharomyces cerevisiae (MeSH)</term><term>Protéines fongiques (effets des médicaments et des substances chimiques)</term><term>Protéines fongiques (génétique)</term><term>RT-PCR (MeSH)</term><term>Recombinaison génétique (MeSH)</term><term>Résistance aux substances (MeSH)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Sirolimus (analogues et dérivés)</term><term>Sirolimus (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Tacrolimus Binding Protein 1A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term><term>Immunosuppressive Agents</term><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Cryptococcus neoformans</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Candida albicans</term><term>Cryptococcus neoformans</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Candida albicans</term><term>Cryptococcus neoformans</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéine 1A de liaison au tacrolimus</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Candida albicans</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Cryptococcus neoformans</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Candida albicans</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines fongiques</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term><term>Immunosuppresseurs</term><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Culture Media</term><term>DNA Primers</term><term>Drug Resistance</term><term>Mutagenesis</term><term>Phosphatidylinositol 3-Kinases</term><term>Recombination, Genetic</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Milieux de culture</term><term>Mutagenèse</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>RT-PCR</term><term>Recombinaison génétique</term><term>Résistance aux substances</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Candida albicans and Cryptococcus neoformans cause both superficial and disseminated infections in humans. Current antifungal therapies for deep-seated infections are limited to amphotericin B, flucytosine, and azoles. A limitation is that commonly used azoles are fungistatic in vitro and in vivo. Our studies address the mechanisms of antifungal activity of the immunosuppressive drug rapamycin (sirolimus) and its analogs with decreased immunosuppressive activity. C. albicans rbp1/rbp1 mutant strains lacking a homolog of the FK506-rapamycin target protein FKBP12 were found to be viable and resistant to rapamycin and its analogs. Rapamycin and analogs promoted FKBP12 binding to the wild-type Tor1 kinase but not to a rapamycin-resistant Tor1 mutant kinase (S1972R). FKBP12 and TOR mutations conferred resistance to rapamycin and its analogs in C. albicans, C. neoformans, and Saccharomyces cerevisiae. Our findings demonstrate the antifungal activity of rapamycin and rapamycin analogs is mediated via conserved complexes with FKBP12 and Tor kinase homologs in divergent yeasts. Taken together with our observations that rapamycin and its analogs are fungicidal and that spontaneous drug resistance occurs at a low rate, these mechanistic findings support continued investigation of rapamycin analogs as novel antifungal agents.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11600372</PMID><DateCompleted><Year>2002</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0066-4804</ISSN><JournalIssue CitedMedium="Print"><Volume>45</Volume><Issue>11</Issue><PubDate><Year>2001</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Antimicrobial agents and chemotherapy</Title><ISOAbbreviation>Antimicrob Agents Chemother</ISOAbbreviation></Journal><ArticleTitle>Rapamycin and less immunosuppressive analogs are toxic to Candida albicans and Cryptococcus neoformans via FKBP12-dependent inhibition of TOR.</ArticleTitle><Pagination><MedlinePgn>3162-70</MedlinePgn></Pagination><Abstract><AbstractText>Candida albicans and Cryptococcus neoformans cause both superficial and disseminated infections in humans. Current antifungal therapies for deep-seated infections are limited to amphotericin B, flucytosine, and azoles. A limitation is that commonly used azoles are fungistatic in vitro and in vivo. Our studies address the mechanisms of antifungal activity of the immunosuppressive drug rapamycin (sirolimus) and its analogs with decreased immunosuppressive activity. C. albicans rbp1/rbp1 mutant strains lacking a homolog of the FK506-rapamycin target protein FKBP12 were found to be viable and resistant to rapamycin and its analogs. Rapamycin and analogs promoted FKBP12 binding to the wild-type Tor1 kinase but not to a rapamycin-resistant Tor1 mutant kinase (S1972R). FKBP12 and TOR mutations conferred resistance to rapamycin and its analogs in C. albicans, C. neoformans, and Saccharomyces cerevisiae. Our findings demonstrate the antifungal activity of rapamycin and rapamycin analogs is mediated via conserved complexes with FKBP12 and Tor kinase homologs in divergent yeasts. Taken together with our observations that rapamycin and its analogs are fungicidal and that spontaneous drug resistance occurs at a low rate, these mechanistic findings support continued investigation of rapamycin analogs as novel antifungal agents.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cruz</LastName><ForeName>M C</ForeName><Initials>MC</Initials><AffiliationInfo><Affiliation>Department of Genetics, The Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Goldstein</LastName><ForeName>A L</ForeName><Initials>AL</Initials></Author><Author ValidYN="Y"><LastName>Blankenship</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Del Poeta</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Perfect</LastName><ForeName>J R</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>McCusker</LastName><ForeName>J H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Bennani</LastName><ForeName>Y L</ForeName><Initials>YL</Initials></Author><Author ValidYN="Y"><LastName>Cardenas</LastName><ForeName>M E</ForeName><Initials>ME</Initials></Author><Author ValidYN="Y"><LastName>Heitman</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>T32 AI007392</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>K01 CA77075</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI41937</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32-AI07392-10</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI44975</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01 AI044975</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antimicrob Agents Chemother</MedlineTA><NlmUniqueID>0315061</NlmUniqueID><ISSNLinking>0066-4804</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003470">Culture Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007166">Immunosuppressive Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C083324">TOR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.2.1.-</RegistryNumber><NameOfSubstance UI="D022061">Tacrolimus Binding Protein 1A</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002176" MajorTopicYN="N">Candida albicans</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003455" MajorTopicYN="N">Cryptococcus neoformans</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004351" MajorTopicYN="N">Drug Resistance</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007166" MajorTopicYN="N">Immunosuppressive Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016296" MajorTopicYN="N">Mutagenesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="Y">Phosphatidylinositol 3-Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011995" MajorTopicYN="N">Recombination, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020123" 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