Deciphering the biosynthetic codes for the potent anti-SARS-CoV cyclodepsipeptide valinomycin in Streptomyces tsusimaensis ATCC 15141.
Identifieur interne : 002235 ( PubMed/Checkpoint ); précédent : 002234; suivant : 002236Deciphering the biosynthetic codes for the potent anti-SARS-CoV cyclodepsipeptide valinomycin in Streptomyces tsusimaensis ATCC 15141.
Auteurs : Yi-Qiang Cheng [États-Unis]Source :
- Chembiochem : a European journal of chemical biology [ 1439-4227 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- biosynthèse : Antibactériens, Valinomycine.
- génétique : Streptomyces.
- métabolisme : Antiviraux, Streptomyces.
- pharmacologie : Antiviraux.
- Animaux, Cellules Vero, Données de séquences moléculaires, Famille multigénique, Gènes bactériens, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Anti-Bacterial Agents (biosynthesis), Antiviral Agents (metabolism), Antiviral Agents (pharmacology), Chlorocebus aethiops, Genes, Bacterial, Molecular Sequence Data, Multigene Family, SARS Virus (drug effects), Streptomyces (genetics), Streptomyces (metabolism), Valinomycin (biosynthesis), Vero Cells.
- MESH :
- chemical , biosynthesis : Anti-Bacterial Agents, Valinomycin.
- chemical , metabolism : Antiviral Agents.
- chemical , pharmacology : Antiviral Agents.
- drug effects : SARS Virus.
- genetics : Streptomyces.
- metabolism : Streptomyces.
- Animals, Chlorocebus aethiops, Genes, Bacterial, Molecular Sequence Data, Multigene Family, Vero Cells.
Abstract
Valinomycin was recently reported to be the most potent agent against severe acute respiratory-syndrome coronavirus (SARS-CoV) in infected Vero E6 cells. Aimed at generating analogues by metabolic engineering, the valinomycin biosynthetic gene cluster has been cloned from Streptomyces tsusimaensis ATCC 15141. Targeted disruption of a nonribosomal peptide synthetase (NRPS) gene abolishes valinomycin production, which confirms its predicted nonribosomal-peptide origin. Sequence analysis of the NRPS system reveals four distinctive modules, two of which contain unusual domain organizations that are presumably involved in the generation of biosynthetic precursors D-alpha-hydroxyisovaleric acid and L-lactic acid. The respective adenylation domains in these two modules contain novel substrate-specificity-conferring codes that might specify for a class of hydroxyl acids for the biosynthesis of the depsipeptide natural products.
DOI: 10.1002/cbic.200500425
PubMed: 16511823
Affiliations:
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pubmed:16511823Le document en format XML
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<front><div type="abstract" xml:lang="en">Valinomycin was recently reported to be the most potent agent against severe acute respiratory-syndrome coronavirus (SARS-CoV) in infected Vero E6 cells. Aimed at generating analogues by metabolic engineering, the valinomycin biosynthetic gene cluster has been cloned from Streptomyces tsusimaensis ATCC 15141. Targeted disruption of a nonribosomal peptide synthetase (NRPS) gene abolishes valinomycin production, which confirms its predicted nonribosomal-peptide origin. Sequence analysis of the NRPS system reveals four distinctive modules, two of which contain unusual domain organizations that are presumably involved in the generation of biosynthetic precursors D-alpha-hydroxyisovaleric acid and L-lactic acid. The respective adenylation domains in these two modules contain novel substrate-specificity-conferring codes that might specify for a class of hydroxyl acids for the biosynthesis of the depsipeptide natural products.</div>
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<ReferenceList><Reference><Citation>Appl Environ Microbiol. 1998 Dec;64(12):4767-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9835560</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Gene. 1992 Jul 1;116(1):43-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1628843</ArticleId>
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</ReferenceList>
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<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Wisconsin</li>
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<tree><country name="États-Unis"><region name="Wisconsin"><name sortKey="Cheng, Yi Qiang" sort="Cheng, Yi Qiang" uniqKey="Cheng Y" first="Yi-Qiang" last="Cheng">Yi-Qiang Cheng</name>
</region>
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</affiliations>
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