Mollisin, an antifungal protein from the chestnut Castanea mollissima.
Identifieur interne : 000462 ( Main/Corpus ); précédent : 000461; suivant : 000463Mollisin, an antifungal protein from the chestnut Castanea mollissima.
Auteurs : K T Chu ; T B NgSource :
- Planta medica [ 0032-0943 ] ; 2003.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Antifungal Agents (administration & dosage), Antifungal Agents (pharmacology), Antifungal Agents (therapeutic use), Fagaceae (MeSH), HIV-1 (drug effects), Humans (MeSH), Microbial Sensitivity Tests (MeSH), Mitosporic Fungi (drug effects), Molecular Sequence Data (MeSH), Naphthoquinones (administration & dosage), Naphthoquinones (chemistry), Naphthoquinones (pharmacology), Naphthoquinones (therapeutic use), Phytotherapy (MeSH), Plant Proteins (administration & dosage), Plant Proteins (chemistry), Plant Proteins (pharmacology), Plant Proteins (therapeutic use), Seeds (MeSH).
- MESH :
- chemical , administration & dosage : Antifungal Agents, Naphthoquinones, Plant Proteins.
- chemical , chemistry : Naphthoquinones, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Naphthoquinones, Plant Proteins.
- chemical , therapeutic use : Antifungal Agents, Naphthoquinones, Plant Proteins.
- drug effects : HIV-1, Mitosporic Fungi.
- Amino Acid Sequence, Fagaceae, Humans, Microbial Sensitivity Tests, Molecular Sequence Data, Phytotherapy, Seeds.
Abstract
The isolation of a protein designated mollisin, with an N-terminal sequence manifesting some similarity to thaumatin-like proteins (TLPs), and possessing a molecular mass of 28 kDa which is higher than those of TLPs, is reported herein from the seeds of the chestnut Castanea mollisima. The protein was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. Mollisin exhibited a molecular mass of 28 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as well as in gel filtration on Superdex 75 by fast protein liquid chromatography. The protein inhibited mycelial growth in Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola, with an IC (50) of 0.83 microM, 6.48 microM and 9.21 microM, respectively. Mollisin displayed a higher antifungal potency than French bean and kiwi fruit TLPs toward F. oxysporum and M. arachidicola. The antifungal activity of mollisin was unaffected by incubation at 40 degrees C for 10 minutes, underwent a decline after incubation at 60 degrees C, and was completely abolished after treatment at 80 degrees C. Mollisin exhibited a more potent inhibitory activity on HIV-1 reverse transcriptase than kiwi fruit TLP.
DOI: 10.1055/s-2003-43216
PubMed: 14598205
Links to Exploration step
pubmed:14598205Le document en format XML
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The protein was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. Mollisin exhibited a molecular mass of 28 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as well as in gel filtration on Superdex 75 by fast protein liquid chromatography. The protein inhibited mycelial growth in Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola, with an IC (50) of 0.83 microM, 6.48 microM and 9.21 microM, respectively. Mollisin displayed a higher antifungal potency than French bean and kiwi fruit TLPs toward F. oxysporum and M. arachidicola. The antifungal activity of mollisin was unaffected by incubation at 40 degrees C for 10 minutes, underwent a decline after incubation at 60 degrees C, and was completely abolished after treatment at 80 degrees C. Mollisin exhibited a more potent inhibitory activity on HIV-1 reverse transcriptase than kiwi fruit TLP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14598205</PMID><DateCompleted><Year>2004</Year><Month>01</Month><Day>28</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0943</ISSN><JournalIssue CitedMedium="Print"><Volume>69</Volume><Issue>9</Issue><PubDate><Year>2003</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Planta medica</Title><ISOAbbreviation>Planta Med</ISOAbbreviation></Journal><ArticleTitle>Mollisin, an antifungal protein from the chestnut Castanea mollissima.</ArticleTitle><Pagination><MedlinePgn>809-13</MedlinePgn></Pagination><Abstract><AbstractText>The isolation of a protein designated mollisin, with an N-terminal sequence manifesting some similarity to thaumatin-like proteins (TLPs), and possessing a molecular mass of 28 kDa which is higher than those of TLPs, is reported herein from the seeds of the chestnut Castanea mollisima. The protein was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. Mollisin exhibited a molecular mass of 28 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as well as in gel filtration on Superdex 75 by fast protein liquid chromatography. The protein inhibited mycelial growth in Fusarium oxysporum, Mycosphaerella arachidicola and Physalospora piricola, with an IC (50) of 0.83 microM, 6.48 microM and 9.21 microM, respectively. Mollisin displayed a higher antifungal potency than French bean and kiwi fruit TLPs toward F. oxysporum and M. arachidicola. The antifungal activity of mollisin was unaffected by incubation at 40 degrees C for 10 minutes, underwent a decline after incubation at 60 degrees C, and was completely abolished after treatment at 80 degrees C. Mollisin exhibited a more potent inhibitory activity on HIV-1 reverse transcriptase than kiwi fruit TLP.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chu</LastName><ForeName>K T</ForeName><Initials>KT</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ng</LastName><ForeName>T B</ForeName><Initials>TB</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta Med</MedlineTA><NlmUniqueID>0066751</NlmUniqueID><ISSNLinking>0032-0943</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009285">Naphthoquinones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>667-92-5</RegistryNumber><NameOfSubstance UI="C010610">mollisin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="N">administration & dosage</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029962" MajorTopicYN="Y">Fagaceae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015497" MajorTopicYN="N">HIV-1</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008826" MajorTopicYN="N">Microbial Sensitivity Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003904" MajorTopicYN="N">Mitosporic Fungi</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009285" MajorTopicYN="N">Naphthoquinones</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="N">administration & dosage</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008517" MajorTopicYN="Y">Phytotherapy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="N">administration & dosage</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012639" MajorTopicYN="N">Seeds</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>11</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>1</Month><Day>30</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>11</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14598205</ArticleId><ArticleId IdType="doi">10.1055/s-2003-43216</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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