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Journal articles on the topic 'Pateamine'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Matthews, James H., David R. Maass, Peter T. Northcote, Paul H. Atkinson, and Paul H. Teesdale-Spittle. "The Cellular Target Specificity of Pateamine A." Zeitschrift für Naturforschung C 68, no. 9-10 (October 1, 2013): 406–15. http://dx.doi.org/10.1515/znc-2013-9-1008.

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The natural product pateamine A (pateamine) from the sponge Mycale hentscheli is active against a wide range of dividing cells and has been shown to inhibit the functions of the eukaryotic initiation factor 4A (eIF4A). We have identifi ed that pateamine is additionally able to modulate the formation of actin fi laments and microtubules in vitro but at higher concentrations than required for inhibition of eIF4A. Cell cycle analysis confi rmed that actin and tubulin are not major mediators of the cellular activity of pateamine. The range of targets identifi ed demonstrates the value of multiple approaches to determining the mode of action of biologically active compounds

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2

Dang, Yongjun, Nancy Kedersha, Woon-Kai Low, Daniel Romo, Myriam Gorospe, Randal Kaufman, Paul Anderson, and Jun O. Liu. "Eukaryotic Initiation Factor 2α-independent Pathway of Stress Granule Induction by the Natural Product Pateamine A." Journal of Biological Chemistry 281, no. 43 (September 2, 2006): 32870–78. http://dx.doi.org/10.1074/jbc.m606149200.

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Stress granules are aggregates of small ribosomal subunits, mRNA, and numerous associated RNA-binding proteins that include several translation initiation factors. Stress granule assembly occurs in the cytoplasm of higher eukaryotic cells under a wide variety of stress conditions, including heat shock, UV irradiation, hypoxia, and exposure to arsenite. Thus far, a unifying principle of eukaryotic initiation factor 2α phosphorylation prior to stress granule formation has been observed from the majority of experimental evidence. Pateamine A, a natural product isolated from marine sponge, was recently reported to inhibit eukaryotic translation initiation and induce the formation of stress granules. In this report, the protein composition and fundamental progression of stress granule formation and disassembly induced by pateamine A was found to be similar to that for arsenite. However, pateamine A-induced stress granules were more stable and less prone to disassembly than those formed in the presence of arsenite. Most significantly, pateamine A induced stress granules independent of eukaryotic initiation factor 2α phosphorylation, suggesting an alternative mechanism of formation from that previously described for other cellular stresses. Taking into account the known inhibitory effect of pateamine A on eukaryotic translation initiation, a model is proposed to account for the induction of stress granules by pateamine A as well as other stress conditions through perturbation of any steps prior to the rejoining of the 60S ribosomal subunit during the entire translation initiation process.

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3

Pattenden, Gerald, Douglas J. Critcher, and Modesto Remuiñán. "Total synthesis of ()-pateamine A, a novel immunosuppressive agent from Mycale sp." Canadian Journal of Chemistry 82, no. 2 (February 1, 2004): 353–65. http://dx.doi.org/10.1139/v03-199.

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A convergent synthesis of the unique thiazole-containing polyene bis-lactone pateamine A (1) isolated from the marine sponge Mycale sp is described. The synthesis features the ubiquitous Stille sp2sp2 coupling reaction to elaborate the E,Z-diene macrolide core 23 and the all-E polyenamine side chain in the natural product. It also highlights the scope for enantiopure sulfinimine intermediates in the synthesis of chiral β-amino ester moieties in complex structures.Key words: pateamine A, immunosuppressive agent from marine sponge Mycale sp, total synthesis, novel 19-membered bis-lactone, thiazole metabolite, polyenamine, Stille reaction, sulfinimines, chiral β-amino esters.

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4

Hemi Cumming, A., Sarah L. Brown, Xu Tao, Claire Cuyamendous, Jessica J. Field, John H. Miller, Joanne E. Harvey, and Paul H. Teesdale-Spittle. "Synthesis of a simplified triazole analogue of pateamine A." Organic & Biomolecular Chemistry 14, no. 22 (2016): 5117–27. http://dx.doi.org/10.1039/c6ob00086j.

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5

Korneeva, Nadejda L. "Translational Dysregulation by Pateamine A." Chemistry & Biology 14, no. 1 (January 2007): 5–7. http://dx.doi.org/10.1016/j.chembiol.2007.01.003.

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6

Kommaraju, Sai Shilpa, Julieta Aulicino, Shruthi Gobbooru, Jing Li, Mingzhao Zhu, Daniel Romo, and Woon-Kai Low. "Investigation of the mechanism of action of a potent pateamine A analog, des-methyl, des-amino pateamine A (DMDAPatA)." Biochemistry and Cell Biology 98, no. 4 (August 2020): 502–10. http://dx.doi.org/10.1139/bcb-2019-0307.

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The natural product pateamineA (PatA) is a highly potent antiproliferative agent. PatA and the simplified analog desmethyl, desamino pateamineA (DMDAPatA) have exhibited cytotoxicity selective for rapidly proliferating cells, and have been shown to inhibit cap-dependent translation initiation through binding to eIF4A (eukaryotic initiation factor 4A) of the eIF4F complex. PatA and DMDAPatA are both known to stimulate the RNA-dependent ATPase, and ATP-dependent RNA helicase activities of eIF4A. The impact of other eIF4F components, eIF4E and eIF4G, on DMDAPatA action were investigated in vitro and in cultured mammalian cells. The perturbation of the eIF4A–eIF4G association was found to be eIF4E- and mRNA cap-dependent. An inhibitory effect on helicase activity of eIF4A was observed when it was part of a complex that mimicked the eIF4F complex. We propose a model of action for DMDAPatA (and by supposition PatA) where the cellular activity of the compound is dependent on an “active” eIF4F complex.

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7

Matthews, James H., David R. Maass, Peter T. Northcote, Paul H. Atkinson, and Paul H. Teesdale-Spittle. "The Cellular Target Specifi city of Pateamine A." Zeitschrift für Naturforschung C 68 (2013): 0406. http://dx.doi.org/10.5560/znc.2013.68c0406.

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8

Kuznetsov, Galina, Qunli Xu, Lori Rudolph-Owen, Karen TenDyke, Junke Liu, Murray Towle, Nanding Zhao, et al. "Potent in vitro and in vivo anticancer activities of des-methyl, des-amino pateamine A, a synthetic analogue of marine natural product pateamine A." Molecular Cancer Therapeutics 8, no. 5 (May 2009): 1250–60. http://dx.doi.org/10.1158/1535-7163.mct-08-1026.

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9

Zhuo, Chun-Xiang, and Alois Fürstner. "Catalysis-Based Total Syntheses of Pateamine A and DMDA-Pat A." Journal of the American Chemical Society 140, no. 33 (July 28, 2018): 10514–23. http://dx.doi.org/10.1021/jacs.8b05094.

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10

Low, Woon-Kai, Yongjun Dang, Tilman Schneider-Poetsch, Zonggao Shi, Nam Song Choi, William C. Merrick, Daniel Romo, and Jun O. Liu. "Inhibition of Eukaryotic Translation Initiation by the Marine Natural Product Pateamine A." Molecular Cell 20, no. 5 (December 2005): 709–22. http://dx.doi.org/10.1016/j.molcel.2005.10.008.

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11

Northcote, Peter T., John W. Blunt, and Murray H. G. Munro. "Pateamine: a potent cytotoxin from the New Zealand Marine sponge, mycale sp." Tetrahedron Letters 32, no. 44 (October 1991): 6411–14. http://dx.doi.org/10.1016/0040-4039(91)80182-6.

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12

Parikh, D., J. Dougan, J. Li, D. Romo, N. J. Moorman, L. M. Graves, and P. R. Graves. "Des-methyl, Des-amino pateamine A, a Synthetic Analogue of Marine Natural Product Pateamine A, Sensitizes Non-small Cell Lung Cancer Cells to Radiation and Enhances BAX Expression." International Journal of Radiation Oncology*Biology*Physics 84, no. 3 (November 2012): S701—S702. http://dx.doi.org/10.1016/j.ijrobp.2012.07.1875.

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13

Dean, Andrea, Thien Nguyen, Nathan Cox, Matthew Cooper, Kristy L. Richards, Thomas C. Shea, Nathaniel Moorman, and Lee Graves. "Investigation of the Novel Anti-Leukemia Effects of the Marine Compound Pateamine A." Blood 120, no. 21 (November 16, 2012): 2437. http://dx.doi.org/10.1182/blood.v120.21.2437.2437.

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Abstract Abstract 2437 Background: Acute myeloid leukemia (AML) remains a devastating disease. This is mainly due to limited treatment options for patients with relapsed or refractory disease and those with FMS-like tyrosine kinase 3 (FLT3) internal tandem duplication (ITD) mutations. FLT3-ITD occurs in approximately a quarter of patients with AML and confers poor prognosis due to high propensity for relapse after remission. The discovery of novel therapies is necessary for cure of AML. Pateamine A (Pat A) is a natural protein translation inhibitor that targets the eukaryotic initiation factor 4A (eIF4A) and inhibits 5'CAP dependent translation. A previous study by Galina Kuznetsov revealed that des-methyl, des-amino Pateamine A (DMDA-Pat A), a synthetic analogue of Pat A, had potent anti-proliferative activity against several human cancer cell lines, including melanoma, colon cancer, non-small cell lung cancer and pre-B acute lymphoid leukemia (Molecular Cancer Therapeutics 2009). The effectiveness of Pat A on AML cells has yet to be elucidated. The primary objective of this study was to determine if Pat A decreased AML FLT3-ITD cell proliferation and caused cell death. The secondary objective was to determine if Pat A decreased AML FLT3-ITD cell protein translation. Lastly, the tertiary objectives were to compare Pat A to AML therapies currently under investigation and in clinical practice and to examine the effects of combination treatments with Pat A on AML FLT3-ITD cells. Methods: Human acute myeloid leukemia MV411 (FLT3-ITD) cells were seeded in the presence of increasing concentrations of DMDA-Pat A. After 48 hours cell proliferation was assessed using MTS assay. To determine if MV411 cells underwent cell death, western blot analysis for PARP-cleavage and fluorometric caspase activation analysis were performed on cell lysates after DMDA -Pat A treatment for 24 hours. Western blot analysis for cell survival regulatory proteins, XIAP, MCL-1, BCL2 and BCL-XL, were performed on treated cell lysates as well. To determine if DMDA-Pat A decreased MV411 protein translation, cells were treated for 3 hours with DMDA-Pat A and labeled with 35S-methionine during last 15 minutes of experiment. Radiolabeled proteins were trichloroacetic acid (TCA) precipitated and measured by scintillation counting. In order to compare DMDA-Pat A to compounds currently in clinical practice, MTS cell proliferation assays were performed on MV411 cells with increasing concentrations of Idarubicin, Cytarabine and Midostaurin (PKC 412; FLT3 inhibitor). Also DMDA-Pat A was compared to Torin, a mammalian target of rapamycin complex (mTORC1/2) inhibitor, which is currently under investigation for treatment of AML. Lastly, MV411 cells were treated with DMDA-Pat A in combination with the above compounds in order to possibly produce synergistic inhibition of cell growth. Results: DMDA-Pat A decreased MV411 cell proliferation with an IC50 of approximately 20 nM. The maximum inhibition of cell growth was achieved at 100nM of DMDA-Pat A. Western blot analyses revealed that MV411 cells underwent cell death as determined by PARP cleavage with 20nM and 100nM of DMDA-Pat A. Fluorometric caspase activation assay revealed an increase in caspase activation with 20nM DMDA-Pat A treatment. Cell survival regulatory proteins XIAP, MCL-1 and BCL-XL were all decreased whereas BCL-2 was unchanged. In comparison to control, MV411 protein translation was decreased by 50% after 20 nM DMDA-Pat A treatment. Idarubicin, Cytarabine, Midostaurin and Torin were all able to decrease MV411 cell proliferation, but the half maximal inhibitory concentrations (IC50) of all four compounds were greater than DMDA-Pat A (Idarubicin IC50 100nm, Cytarabine IC50 30nm, Midostaurin IC50 125nm and Torin IC50 60 nm). Lastly, there was no synergistic inhibition of cell growth with DMDA-Pat A and any of the above four compounds, but DMDA-Pat A in combination with Idarubicin produced additive inhibition of cell growth. Conclusion: DMDA-Pat A decreases proliferation of FLT3-ITD MV411 cells by reducing cell survival proteins and inducing apoptosis at low concentrations. DMDA-Pat A was determined to be effective at concentrations lower than another protein synthesis inhibitor (Torin) or other cytotoxic agents (Idarubicin, Cytarabine, Midostaurin). In combination with other cytotoxic drugs, DMDA-Pat A could be a potential treatment option for AML patients with FLT3-ITD mutations. Disclosures: No relevant conflicts of interest to declare.

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14

Bordeleau, Marie-Eve, Regina Cencic, Lisa Lindqvist, Monika Oberer, Peter Northcote, Gerhard Wagner, and Jerry Pelletier. "RNA-Mediated Sequestration of the RNA Helicase eIF4A by Pateamine A Inhibits Translation Initiation." Chemistry & Biology 13, no. 12 (December 2006): 1287–95. http://dx.doi.org/10.1016/j.chembiol.2006.10.005.

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15

González-Almela, Esther, Miguel Angel Sanz, Manuel García-Moreno, Peter Northcote, Jerry Pelletier, and Luis Carrasco. "Differential action of pateamine A on translation of genomic and subgenomic mRNAs from Sindbis virus." Virology 484 (October 2015): 41–50. http://dx.doi.org/10.1016/j.virol.2015.05.002.

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16

Critcher, Douglas J., and Gerald Pattenden. "Synthetic studies towards pateamine, a novel thiazole-based 19-membered bis-lactone from Mycale sp." Tetrahedron Letters 37, no. 50 (December 1996): 9107–10. http://dx.doi.org/10.1016/s0040-4039(96)02098-9.

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17

Rzasa, Robert M., Helene A. Shea, and Daniel Romo. "Total Synthesis of the Novel, Immunosuppressive Agent (−)-Pateamine A fromMycalesp. Employing a β-Lactam-Based Macrocyclization." Journal of the American Chemical Society 120, no. 3 (January 1998): 591–92. http://dx.doi.org/10.1021/ja973549f.

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18

Dang, Yongjun, Woon-Kai Low, Jing Xu, Niels H. Gehring, Harry C. Dietz, Daniel Romo, and Jun O. Liu. "Inhibition of Nonsense-mediated mRNA Decay by the Natural Product Pateamine A through Eukaryotic Initiation Factor 4AIII." Journal of Biological Chemistry 284, no. 35 (July 1, 2009): 23613–21. http://dx.doi.org/10.1074/jbc.m109.009985.

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19

Remuiñán, Modesto J., and Gerald Pattenden. "Total synthesis of ()-pateamine, a novel polyene bis-macrolide with immunosuppressive activity from the sponge Mycale sp." Tetrahedron Letters 41, no. 38 (September 2000): 7367–71. http://dx.doi.org/10.1016/s0040-4039(00)01241-7.

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20

Low, Woon-Kai, Jing Li, Mingzhao Zhu, Sai Shilpa Kommaraju, Janki Shah-Mittal, Ken Hull, Jun O. Liu, and Daniel Romo. "Second-generation derivatives of the eukaryotic translation initiation inhibitor pateamine A targeting eIF4A as potential anticancer agents." Bioorganic & Medicinal Chemistry 22, no. 1 (January 2014): 116–25. http://dx.doi.org/10.1016/j.bmc.2013.11.046.

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21

CRITCHER, D. J., and G. PATTENDEN. "ChemInform Abstract: Synthetic Studies Towards Pateamine, a Novel Thiazole-Based 19- Membered Bis-lactone from Mycale sp." ChemInform 28, no. 15 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199715224.

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22

Romo, Daniel, Robert M. Rzasa, Helene A. Shea, Kaapjoo Park, Joseph M. Langenhan, Luo Sun, Alexander Akhiezer, and Jun O. Liu. "Total Synthesis and Immunosuppressive Activity of (−)-Pateamine A and Related Compounds: Implementation of a β-Lactam-Based Macrocyclization." Journal of the American Chemical Society 120, no. 47 (December 1998): 12237–54. http://dx.doi.org/10.1021/ja981846u.

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23

Naineni, Sai Kiran, Jason Liang, Kenneth Hull, Regina Cencic, Mingzhao Zhu, Peter Northcote, Paul Teesdale-Spittle, Daniel Romo, Bhushan Nagar, and Jerry Pelletier. "Functional mimicry revealed by the crystal structure of an eIF4A:RNA complex bound to the interfacial inhibitor, desmethyl pateamine A." Cell Chemical Biology 28, no. 6 (June 2021): 825–34. http://dx.doi.org/10.1016/j.chembiol.2020.12.006.

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24

Low, Woon-Kai, Yongjun Dang, Shridhar Bhat, Daniel Romo, and Jun O. Liu. "Substrate-Dependent Targeting of Eukaryotic Translation Initiation Factor 4A by Pateamine A: Negation of Domain-Linker Regulation of Activity." Chemistry & Biology 14, no. 6 (June 2007): 715–27. http://dx.doi.org/10.1016/j.chembiol.2007.05.012.

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25

Remuinan, Modesto J., and Gerald Pattenden. "ChemInform Abstract: Total Synthesis of (-)-Pateamine, a Novel Polyene Bis-macrolide with Immunosuppressive Activity from the Sponge Mycale sp." ChemInform 31, no. 50 (December 12, 2000): no. http://dx.doi.org/10.1002/chin.200050222.

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26

Xu, Tao, Claire Cuyamendous, Sarah L. Brown, Sarah K. Andreassend, Hemi Cumming, Gary B. Evans, Paul H. Teesdale-Spittle, and Joanne E. Harvey. "Gold(I)-catalyzed, one-pot, oxidative formation of 2,4-disubstituted thiazoles: Application to the synthesis of a pateamine-related macrodiolide." Tetrahedron 88 (May 2021): 132109. http://dx.doi.org/10.1016/j.tet.2021.132109.

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27

Romo, Daniel, Robert M. Rzasa, Helene A. Shea, Kaapjoo Park, Joseph M. Langenhan, Luo Sun, Alexander Akhiezer, and Jun O. Liu. "ChemInform Abstract: Total Synthesis of Immunosuppressive Activity of (-)-Pateamine A and Related Compounds: Implementation of a β-Lactam-Based Macrocyclization." ChemInform 30, no. 18 (June 16, 2010): no. http://dx.doi.org/10.1002/chin.199918232.

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28

RZASA, R. M., H. A. SHEA, and D. ROMO. "ChemInform Abstract: Total Synthesis of the Novel, Immunosuppressive Agent (-)-Pateamine A from Mycale sp. Employing a β-Lactam-Based Macrocyclization." ChemInform 29, no. 24 (June 22, 2010): no. http://dx.doi.org/10.1002/chin.199824204.

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29

Zhuo, Chun-Xiang, and Alois Fürstner. "Concise Synthesis of a Pateamine A Analogue with In Vivo Anticancer Activity Based on an Iron-Catalyzed Pyrone Ring Opening/Cross-Coupling." Angewandte Chemie International Edition 55, no. 20 (April 8, 2016): 6051–56. http://dx.doi.org/10.1002/anie.201602125.

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30

Zhuo, Chun-Xiang, and Alois Fürstner. "Concise Synthesis of a Pateamine A Analogue with In Vivo Anticancer Activity Based on an Iron-Catalyzed Pyrone Ring Opening/Cross-Coupling." Angewandte Chemie 128, no. 20 (April 8, 2016): 6155–60. http://dx.doi.org/10.1002/ange.201602125.

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31

Romo, Daniel, Nam Song Choi, Shukun Li, Ingrid Buchler, Zonggao Shi, and Jun O. Liu. "Evidence for Separate Binding and Scaffolding Domains in the Immunosuppressive and Antitumor Marine Natural Product, Pateamine A: Design, Synthesis, and Activity Studies Leading to a Potent Simplified Derivative." Journal of the American Chemical Society 126, no. 34 (September 2004): 10582–88. http://dx.doi.org/10.1021/ja040065s.

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32

Pal, Ipsita, Yu Ri Kim, Sohani Das Sharma, Prabhjot S. Mundi, Andre M. Grilo, Luke E. Berchowitz, Mingzhao Zhu, et al. "Targeting eIF4A Using MZ-735 Potently Induces Cell Death in Lymphoma Cells and Rapidly Represses mRNA Translation at the Global Level and in C-MYC and Other Oncogenes." Blood 134, Supplement_1 (November 13, 2019): 4067. http://dx.doi.org/10.1182/blood-2019-131816.

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Introduction: Dysregulated C-MYC signaling is associated with the pathogenesis and poor survival in aggressive lymphomas such as diffuse large B cell lymphoma (DLBCL). Despite intense investigation, direct inhibitors of C-MYC have not yet advanced to the clinic. Various structural elements, such as TOP (terminal oligopyrimidine tract) motif, guanine quartet (CGG) 4 motif, and polypurine sequences (AGAGAG), have been shown to impart high level of dependence on eukaryotic initiation factor 4F (eIF4F). The eIF4F is comprised of 3 subunits, including the mRNA 5ʹ-cap-binding subunit eIF4E, the large scaffolding subunit eIF4G, and the RNA helicase subunit eIF4A. In the current project, we have investigated targeting eIF4A as a novel therapeutic strategy in lymphoma. Pateamine A (PatA) is a natural product originally isolated from a New Zealand marine sponge, Mycale sp. DMDA-PatA, a first generation PatA analogue, has demonstrated in vivo activity in xenograft cancer models. DMDA-PatA acts by decreasing the interaction between eIF4A and eIF4G that specifically inhibits cap dependent translation. MZ-735 is a recently developed PatA analogue that is more potent than DMDA-PatA and less protein bound. Materials and Methods: MZ-735 was synthesized at the CPRIT Synthesis and Drug-Lead Discovery Laboratory at Baylor University. Cytotoxicity was evaluated in diffuse large B cell and Mantle cell lymphoma cell lines using CellTiter-Glo (Promega®). Western blot analysis was performed for the expressions of oncogenes. Global translation was determined using surface sensing of translation (SUnSET) assay and Polysome profile followed by Western blotting and qPCR. RNA sequencing (RNA-seq) was carried out on drug versus dimethyl sulfoxide (DMSO)-treated cells in DLBCL and MCL. An unbiased proteomics analysis was performed using TMT mass spectrometry. Omics data were analyzed by gene set enrichment analysis (GSEA) and Virtual Inference of Protein-activity by Enriched Regulon (VIPER) analysis. Results: MZ-735 were studied in 13 lymphoma cell lines. MZ-735 exhibited concentration- and time-dependent cytotoxicity in lymphoma cell lines at low nanomolar concentrations and showed minimal toxicity in normal PBMC cells. MZ-735 potently inhibits polysome formation, global protein synthesis and inhibits oncogene such as C-Myc and Cyclin D1 in DLBCL and MCL cells. An unbiased quantitative proteomics analysis was carried out to identify the immediate consequence of MZ-735 during a short exposure time of 3 hours. More than 5000 proteins were detected, of which 132 proteins were upregualated and 119 proteins were down regulated by more than twofold after MZ-735 treatment (P < 0.05; fold change, >2). Enrichment analysis suggested that Cancer hallmark proteins such as E2F target proteins, G2/M check point proteins and mitotic spindle proteins were highly enriched among these depleted proteins and the most affected downregulated pathways are cell cycle, cell division and chromosome segregation pathway. We are currently conducting RNAseq to determine whether the mRNA level change in the same or opposite direction as the protein level for any given gene across the genome. Furthermore, we will conduct proteomics and RNAseq in samples treated for longer time points, as the short exposure (3h) favors discovery of depleted proteins with very short half-lives. Conclusion: These results demonstrate that the PatA analogue MZ-735 can potently inhibit the translational apparatus in lymphoma. MZ-735 inhibits metabolic pathways required for cancer progression, leading to growth arrest and apoptosis in the lymphoma cells. MZ-735 and other eIF4A inhibitors represent a promising new class of anti-neoplastic agents, which may be particularly useful for silencing undruggable oncogenes such as C-MYC. Deep insights into the translational responses to eIF4A inhibitors at the single gene level will inform future development of this class of anti-neoplastic agents. Disclosures O'Connor: Allos Therapeutics: Consultancy; Acetylon Pharma: Other: Travel expenses, Research Funding; Celgene: Research Funding; Millenium: Consultancy, Honoraria, Other: Travel expenses, Research Funding; Mundipharma: Consultancy, Honoraria, Other: Travel expenses, Research Funding; Novartis: Consultancy, Honoraria; Roche: Research Funding; Seattle Genetics, Inc.: Consultancy, Other: Travel expenses, Research Funding; Spectrum Pharma: Consultancy, Other: Travel expenses, Research Funding.

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33

Rzasa, R. "Structural and Synthetic Studies of the Pateamines: Synthesis and Absolute Configuration of the Hydroxydienoate Fragment." Tetrahedron Letters 36, no. 30 (July 24, 1995): 5307–10. http://dx.doi.org/10.1016/00404-0399(50)10219-.

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34

Rust, Michael, Eric J. N. Helfrich, Michael F. Freeman, Pakjira Nanudorn, Christopher M. Field, Christian Rückert, Tomas Kündig, et al. "A multiproducer microbiome generates chemical diversity in the marine sponge Mycale hentscheli." Proceedings of the National Academy of Sciences 117, no. 17 (April 14, 2020): 9508–18. http://dx.doi.org/10.1073/pnas.1919245117.

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Bacterial specialized metabolites are increasingly recognized as important factors in animal–microbiome interactions: for example, by providing the host with chemical defenses. Even in chemically rich animals, such compounds have been found to originate from individual members of more diverse microbiomes. Here, we identified a remarkable case of a moderately complex microbiome in the sponge host Mycale hentscheli in which multiple symbionts jointly generate chemical diversity. In addition to bacterial pathways for three distinct polyketide families comprising microtubule-inhibiting peloruside drug candidates, mycalamide-type contact poisons, and the eukaryotic translation-inhibiting pateamines, we identified extensive biosynthetic potential distributed among a broad phylogenetic range of bacteria. Biochemical data on one of the orphan pathways suggest a previously unknown member of the rare polytheonamide-type cytotoxin family as its product. Other than supporting a scenario of cooperative symbiosis based on bacterial metabolites, the data provide a rationale for the chemical variability of M. hentscheli and could pave the way toward biotechnological peloruside production. Most bacterial lineages in the compositionally unusual sponge microbiome were not known to synthesize bioactive metabolites, supporting the concept that microbial dark matter harbors diverse producer taxa with as yet unrecognized drug discovery potential.

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35

RZASA, R. M., D. ROMO, D. J. STIRLING, J. W. BLUNT, and M. H. G. MUNRO. "ChemInform Abstract: Structural and Synthetic Studies of the Pateamines: Synthesis and Absolute Configuration of the Hydroxydienoate Fragment." ChemInform 26, no. 44 (August 17, 2010): no. http://dx.doi.org/10.1002/chin.199544268.

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36

"Synthesis of (–)-Pateamine A." Synfacts 14, no. 11 (October 18, 2018): 1114. http://dx.doi.org/10.1055/s-0037-1611234.

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37

Low, Woon‐Kai, Yongjun Dang, Tilman Schneider‐Poetsch, Zonggao Shi, Nam Song Choi, William C. Merrick, Daniel Romo, and Jun O. Liu. "Inhibition of Eukaryotic Translation Initiation by the Natural Product Pateamine A." FASEB Journal 20, no. 5 (March 2006). http://dx.doi.org/10.1096/fasebj.20.5.lb46-a.

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38

Di Marco, Sergio, Anne Cammas, Xian Jin Lian, Erzsebet Nagy Kovacs, Jennifer F. Ma, Derek T. Hall, Rachid Mazroui, John Richardson, Jerry Pelletier, and Imed Eddine Gallouzi. "The translation inhibitor pateamine A prevents cachexia-induced muscle wasting in mice." Nature Communications 3, no. 1 (January 2012). http://dx.doi.org/10.1038/ncomms1899.

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39

Pattenden, Gerald, Douglas J. Critcher, and Modesto Remuinan. "Total Synthesis of (-)-Pateamine A, a Novel Immunosuppressive Agent from Mycale sp." ChemInform 35, no. 34 (August 24, 2004). http://dx.doi.org/10.1002/chin.200434238.

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"Towards Pateamine. A Comparison of Palladium-catalysed sp2-sp2Coupling Protocols to Polyene Macrolides." Synlett 2000, no. 11 (2000): 1661–63. http://dx.doi.org/10.1055/s-2000-7930.

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Popa, Alexandra, Kevin Lebrigand, Pascal Barbry, and Rainer Waldmann. "Pateamine A-sensitive ribosome profiling reveals the scope of translation in mouse embryonic stem cells." BMC Genomics 17, no. 1 (January 14, 2016). http://dx.doi.org/10.1186/s12864-016-2384-0.

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KOMMARAJU, SAI SHILPA, Jing Li, Mingzhao Zhu, Daniel Romo, and Woon‐Kai Low. "In vitro structure/activity relationship studies of second generation derivatives of the translation initiation inhibitor desmethyl, desamino‐Pateamine A." FASEB Journal 27, S1 (April 2013). http://dx.doi.org/10.1096/fasebj.27.1_supplement.lb69.

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Storey, Mathew A., Sarah K. Andreassend, Joe Bracegirdle, Alistair Brown, Robert A. Keyzers, David F. Ackerley, Peter T. Northcote, and Jeremy G. Owen. "Metagenomic Exploration of the Marine Sponge Mycale hentscheli Uncovers Multiple Polyketide-Producing Bacterial Symbionts." mBio 11, no. 2 (March 24, 2020). http://dx.doi.org/10.1128/mbio.02997-19.

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Abstract:

ABSTRACT Marine sponges have been a prolific source of unique bioactive compounds that are presumed to act as a deterrent to predation. Many of these compounds have potential therapeutic applications; however, the lack of efficient and sustainable synthetic routes frequently limits clinical development. Here, we describe a metagenomic investigation of Mycale hentscheli, a chemically gifted marine sponge that possesses multiple distinct chemotypes. We applied shotgun metagenomic sequencing, hybrid assembly of short- and long-read data, and metagenomic binning to obtain a comprehensive picture of the microbiome of five specimens, spanning three chemotypes. Our data revealed multiple producing species, each having relatively modest secondary metabolomes, that contribute collectively to the chemical arsenal of the holobiont. We assembled complete genomes for multiple new genera, including two species that produce the cytotoxic polyketides pateamine and mycalamide, as well as a third high-abundance symbiont harboring a proteusin-type biosynthetic pathway that appears to encode a new polytheonamide-like compound. We also identified an additional 188 biosynthetic gene clusters, including a pathway for biosynthesis of peloruside. These results suggest that multiple species cooperatively contribute to defensive symbiosis in M. hentscheli and reveal that the taxonomic diversity of secondary-metabolite-producing sponge symbionts is larger and richer than previously recognized. IMPORTANCE Mycale hentscheli is a marine sponge that is rich in bioactive small molecules. Here, we use direct metagenomic sequencing to elucidate highly complete and contiguous genomes for the major symbiotic bacteria of this sponge. We identify complete biosynthetic pathways for the three potent cytotoxic polyketides which have previously been isolated from M. hentscheli. Remarkably, and in contrast to previous studies of marine sponges, we attribute each of these metabolites to a different producing microbe. We also find that the microbiome of M. hentscheli is stably maintained among individuals, even over long periods of time. Collectively, our data suggest a cooperative mode of defensive symbiosis in which multiple symbiotic bacterial species cooperatively contribute to the defensive chemical arsenal of the holobiont.

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Kommaraju, Sai Shilpa, Julieta Aulicino, Jing Li, Mingzhao Zhu, Daniel Romo, and Woon‐Kai Low. "Re‐evaluation of desmethyl, desamino‐PateamineA targeting of eukaryotic translation initiation factor 4F (975.2)." FASEB Journal 28, S1 (April 2014). http://dx.doi.org/10.1096/fasebj.28.1_supplement.975.2.

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