Butenolide inhibits marine fouling by altering the primary metabolism of three target organisms

Handle URI:
http://hdl.handle.net/10754/575561
Title:
Butenolide inhibits marine fouling by altering the primary metabolism of three target organisms
Authors:
Zhang, Yifan; Zhang, Huoming ( 0000-0001-5416-0358 ) ; He, Lisheng; Liu, Changdong; Xü, Ying; Qian, Peiyuan
Abstract:
Butenolide is a very promising antifouling compound that inhibits ship hull fouling by a variety of marine organisms, but its antifouling mechanism was previously unknown. Here we report the first study of butenolides molecular targets in three representative fouling organisms. In the barnacle Balanus (=Amphibalanus) amphitrite, butenolide bound to acetyl-CoA acetyltransferase 1 (ACAT1), which is involved in ketone body metabolism. Both the substrate and the product of ACAT1 increased larval settlement under butenolide treatment, suggesting its functional involvement. In the bryozoan Bugula neritina, butenolide bound to very long chain acyl-CoA dehydrogenase (ACADVL), actin, and glutathione S-transferases (GSTs). ACADVL is the first enzyme in the very long chain fatty acid β-oxidation pathway. The inhibition of this primary pathway for energy production in larvae by butenolide was supported by the finding that alternative energy sources (acetoacetate and pyruvate) increased larval attachment under butenolide treatment. In marine bacterium Vibrio sp. UST020129-010, butenolide bound to succinyl-CoA synthetase β subunit (SCSβ) and inhibited bacterial growth. ACAT1, ACADVL, and SCSβ are all involved in primary metabolism for energy production. These findings suggest that butenolide inhibits fouling by influencing the primary metabolism of target organisms. © 2012 American Chemical Society.
KAUST Department:
KAUST Global Collaborative Research Program; Biosciences Core Lab; Core Labs
Publisher:
American Chemical Society (ACS)
Journal:
ACS Chemical Biology
Issue Date:
15-Jun-2012
DOI:
10.1021/cb200545s
PubMed ID:
22458453
Type:
Article
ISSN:
15548929
Sponsors:
We thank Y. Zhang and J. Sun for their help in UPLC-MS/MS analysis; S. Dash for her help in Vibrio sp. UST020129-010 bioassays and cultures; Z. F. Chen and H. Wang for their help in RNA extraction, cDNA synthesis, and real-time PCR analysis; Y. H. Wong for his help in bugula sample collection; J. P. Ren, P. Chen, H. S. Wong, and R. Ko for their help in thiolase characterization; and S. Bougouffa, K. Matsumura, A. Wu, and J. R. Wu for their helpful comments on a draft of this manuscript. This study was supported by a grant from China Ocean Mineral Resources Research and Development (DY125-15-T-02), a joint research grant from the RGC of the HKSAR and the NSFC of China (N_HKUST602/09), and an award (SA-C0040/UK-C0016) from the King Abdullah University of Science and Technology to P. Y. Qian.
Appears in Collections:
Articles; Biosciences Core Lab

Full metadata record

DC FieldValue Language
dc.contributor.authorZhang, Yifanen
dc.contributor.authorZhang, Huomingen
dc.contributor.authorHe, Lishengen
dc.contributor.authorLiu, Changdongen
dc.contributor.authorXü, Yingen
dc.contributor.authorQian, Peiyuanen
dc.date.accessioned2015-08-24T08:32:54Zen
dc.date.available2015-08-24T08:32:54Zen
dc.date.issued2012-06-15en
dc.identifier.issn15548929en
dc.identifier.pmid22458453en
dc.identifier.doi10.1021/cb200545sen
dc.identifier.urihttp://hdl.handle.net/10754/575561en
dc.description.abstractButenolide is a very promising antifouling compound that inhibits ship hull fouling by a variety of marine organisms, but its antifouling mechanism was previously unknown. Here we report the first study of butenolides molecular targets in three representative fouling organisms. In the barnacle Balanus (=Amphibalanus) amphitrite, butenolide bound to acetyl-CoA acetyltransferase 1 (ACAT1), which is involved in ketone body metabolism. Both the substrate and the product of ACAT1 increased larval settlement under butenolide treatment, suggesting its functional involvement. In the bryozoan Bugula neritina, butenolide bound to very long chain acyl-CoA dehydrogenase (ACADVL), actin, and glutathione S-transferases (GSTs). ACADVL is the first enzyme in the very long chain fatty acid β-oxidation pathway. The inhibition of this primary pathway for energy production in larvae by butenolide was supported by the finding that alternative energy sources (acetoacetate and pyruvate) increased larval attachment under butenolide treatment. In marine bacterium Vibrio sp. UST020129-010, butenolide bound to succinyl-CoA synthetase β subunit (SCSβ) and inhibited bacterial growth. ACAT1, ACADVL, and SCSβ are all involved in primary metabolism for energy production. These findings suggest that butenolide inhibits fouling by influencing the primary metabolism of target organisms. © 2012 American Chemical Society.en
dc.description.sponsorshipWe thank Y. Zhang and J. Sun for their help in UPLC-MS/MS analysis; S. Dash for her help in Vibrio sp. UST020129-010 bioassays and cultures; Z. F. Chen and H. Wang for their help in RNA extraction, cDNA synthesis, and real-time PCR analysis; Y. H. Wong for his help in bugula sample collection; J. P. Ren, P. Chen, H. S. Wong, and R. Ko for their help in thiolase characterization; and S. Bougouffa, K. Matsumura, A. Wu, and J. R. Wu for their helpful comments on a draft of this manuscript. This study was supported by a grant from China Ocean Mineral Resources Research and Development (DY125-15-T-02), a joint research grant from the RGC of the HKSAR and the NSFC of China (N_HKUST602/09), and an award (SA-C0040/UK-C0016) from the King Abdullah University of Science and Technology to P. Y. Qian.en
dc.publisherAmerican Chemical Society (ACS)en
dc.titleButenolide inhibits marine fouling by altering the primary metabolism of three target organismsen
dc.typeArticleen
dc.contributor.departmentKAUST Global Collaborative Research Programen
dc.contributor.departmentBiosciences Core Laben
dc.contributor.departmentCore Labsen
dc.identifier.journalACS Chemical Biologyen
dc.contributor.institutionDepartment of Biology, Hong Kong Baptist University, Hong Kong, Hong Kongen
dc.contributor.institutionDivision of Life Science, Hong Kong University of Science and Technology, Hong Kong, Hong Kongen
kaust.authorZhang, Huomingen
kaust.authorZhang, Yifanen
kaust.authorHe, Lishengen
kaust.authorXü, Yingen
kaust.authorQian, Peiyuanen
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