TY - JOUR A1 - Baraza, Lilechi D. A1 - Neser, Wekesa A1 - Jackson, Korir Cheruiyot A1 - Fredrick, Juma B. A1 - Dennis, Ochieno A1 - Wairimu, Kamau R. A1 - Keya, Aggrey Osogo A1 - Heydenreich, Matthias T1 - Antimicrobial Coumarins from the Oyster Culinary-Medicinal Mushroom, Pleurotus ostreatus (Agaricomycetes), from Kenya JF - International journal of medicinal mushrooms N2 - Pleurotus ostreatus has been widely used as food because of its nutritional and medicinal properties. These have been attributed to the presence of macronutrients, minerals, vitamins, and amino acids, among other secondary metabolites. There are, however, few reports on the antimicrobial activities of different classes of purified compounds from P. ostreatus. This led to the current study, the objective of which was to chemically characterize the antibiotic activities of P. ()streams against selected human pathogenic bacteria and endophytic fungi. Chemical structures were determined using spectroscopic methods and by comparison with values of related structures reported in the literature. Pure compounds from P. ostreatus were tested in vitro against pathogenic bacteria (Staphylococcus aureus and Escherichia coli) and endophytic fungi (Pencillium digitatum and Fusarium prolferatum). A new compound, (E)-5,7-dimethoxy-6-(3-methylbuta-1,3-dienyl)-2H-chromen-2-one (5-methoxy-(E)-suberodiene) (compound 2), along with ergosterol (compound I.) and 5,7-dimethoxy-6-(3-methylbut-2-enyl)-2H-chromen-2-one (toddaculin; compound 3), were isolated from the fruiting bodies of P. ostreatus. The growth of S. aureus,E proliferatum, and P. digitatum colonies was inhibited in media containing compound 2, with minimum inhibitory concentrations closely comparable to those of conventional antibiotics. KW - Escherichia coli KW - Fusarium proliferatum KW - medicinal mushrooms KW - Penicillium digitatum KW - Pleurotus ostreatus KW - Staphylococcus aureus Y1 - 2016 U6 - https://doi.org/10.1615/IntJMedMushrooms.v18.i10.60 SN - 1521-9437 SN - 1940-4344 VL - 18 SP - 905 EP - 913 PB - Begell House CY - Danbury ER - TY - JOUR A1 - Bartholomäus, Alexander A1 - Fedyunin, Ivan A1 - Feist, Peter A1 - Sin, Celine A1 - Zhang, Gong A1 - Valleriani, Angelo A1 - Ignatova, Zoya T1 - Bacteria differently regulate mRNA abundance to specifically respond to various stresses JF - Geology N2 - Environmental stress is detrimental to cell viability and requires an adequate reprogramming of cellular activities to maximize cell survival. We present a global analysis of the response of Escherichia coli to acute heat and osmotic stress. We combine deep sequencing of total mRNA and ribosome-protected fragments to provide a genome-wide map of the stress response at transcriptional and translational levels. For each type of stress, we observe a unique subset of genes that shape the stress-specific response. Upon temperature upshift, mRNAs with reduced folding stability up-and downstream of the start codon, and thus with more accessible initiation regions, are translationally favoured. Conversely, osmotic upshift causes a global reduction of highly translated transcripts with high copy numbers, allowing reallocation of translation resources to not degraded and newly synthesized mRNAs. KW - transcription KW - translation KW - deep sequencing KW - Escherichia coli KW - copy numbers Y1 - 2016 U6 - https://doi.org/10.1098/rsta.2015.0069 SN - 1364-503X SN - 1471-2962 VL - 374 PB - Royal Society CY - London ER - TY - GEN A1 - Connor, Daniel Oliver A1 - Zantow, Jonas A1 - Hust, Michael A1 - Bier, Frank Fabian A1 - von Nickisch-Rosenegk, Markus T1 - Identification of novel immunogenic proteins of Neisseria gonorrhoeae by phage display T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Neisseria gonorrhoeae is one of the most prevalent sexually transmitted diseases worldwide with more than 100 million new infections per year. A lack of intense research over the last decades and increasing resistances to the recommended antibiotics call for a better understanding of gonococcal infection, fast diagnostics and therapeutic measures against N. gonorrhoeae. Therefore, the aim of this work was to identify novel immunogenic proteins as a first step to advance those unresolved problems. For the identification of immunogenic proteins, pHORF oligopeptide phage display libraries of the entire N. gonorrhoeae genome were constructed. Several immunogenic oligopeptides were identified using polyclonal rabbit antibodies against N. gonorrhoeae. Corresponding full-length proteins of the identified oligopeptides were expressed and their immunogenic character was verified by ELISA. The immunogenic character of six proteins was identified for the first time. Additional 13 proteins were verified as immunogenic proteins in N. gonorrhoeae. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 541 KW - proteomic analysis KW - vaccine antigens KW - gene-expression KW - Mycobacterium tuberculosis KW - antimicrobial resistance KW - recombinant antibodies KW - Salmonella Thyphimurium KW - untreatable Gonorrhea KW - multidrug-resistant KW - Escherichia coli Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-411077 SN - 1866-8372 IS - 541 ER - TY - GEN A1 - Yan, Robert A1 - Friemel, Martin A1 - Aloisi, Claudia A1 - Huynen, Martijn A1 - Taylor, Ian A. A1 - Leimkühler, Silke A1 - Pastore, Annalisa T1 - The eukaryotic-specific Isd11 is a complex- orphan protein with ability to bind the prokaryotic IscS T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - The eukaryotic protein Isd11 is a chaperone that binds and stabilizes the central component of the essential metabolic pathway responsible for formation of iron-sulfur clusters in mitochondria, the desulfurase Nfs1. Little is known about the exact role of Isd11. Here, we show that human Isd11 (ISD11) is a helical protein which exists in solution as an equilibrium between monomer, dimeric and tetrameric species when in the absence of human Nfs1 (NFS1). We also show that, surprisingly, recombinant ISD11 expressed in E. coli co-purifies with the bacterial orthologue of NFS1, IscS. Binding is weak but specific suggesting that, despite the absence of Isd11 sequences in bacteria, there is enough conservation between the two desulfurases to retain a similar mode of interaction. This knowledge may inform us on the conservation of the mode of binding of Isd11 to the desulfurase. We used evolutionary evidence to suggest Isd11 residues involved in the interaction. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 551 KW - sulfur cluster formation KW - Escherichia coli KW - cysteine desulfurase KW - interacting protein KW - bacterial frataxin KW - statistical-model KW - biogenesis KW - biosynthesis KW - NFS1 KW - deficiency Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-411906 SN - 1866-8372 IS - 551 ER -