Schalk Felix, Fricke Janis, Um Soohyun, Conlon Benjamin H, Maus Hannah, Jäger Nils, Heinzel Thorsten, Schirmeister Tanja, Poulsen Michael, Beemelmanns Christine
Chemical Biology of Microbe-Host Interactions, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute (HKI) Beutenbergstraße 11a 07745 Jena Germany
Section for Ecology and Evolution, Department of Biology, University of Copenhagen Universitetsparken 15 2100 Copenhagen East Denmark.
RSC Adv. 2021 May 24;11(31):18748-18756. doi: 10.1039/d1ra00997d.
Targeted HRMS-GNPS-based metabolomic analysis of sp. X187, a fungal antagonist of the fungus-growing termite symbiosis, resulted in the identification of two lipopeptidic congeners of xylacremolides, named xylacremolide C and D, which are built from d-phenylalanine, l-proline and an acetyl-CoA starter unit elongated by four malonyl-CoA derived ketide units. The putative gene cluster was identified from a draft genome generated by Illumina and PacBio sequencing and RNAseq studies. Biological activities of xylacremolide A and B were evaluated and revealed weak histone deacetylase inhibitory (HDACi) and antifungal activities, as well as moderate protease inhibition activity across a panel of nine human, viral and bacterial proteases.
基于靶向高分辨质谱-全球天然产物社会分子网络（HRMS-GNPS）对共生菌白蚁的真菌拮抗剂X187菌株进行代谢组学分析，结果鉴定出两种木霉菌内酯脂肽类同系物，命名为木霉菌内酯C和D，它们由d-苯丙氨酸、l-脯氨酸和一个由四个丙二酰辅酶A衍生的聚酮单元延长的乙酰辅酶A起始单元构成。通过Illumina和PacBio测序以及RNAseq研究生成的基因组草图鉴定出了推定的基因簇。对木霉菌内酯A和B的生物活性进行了评估，结果显示其具有较弱的组蛋白脱乙酰酶抑制（HDACi）和抗真菌活性，以及对一组九种人类、病毒和细菌蛋白酶的中等程度的蛋白酶抑制活性。
