نتایج جستجو برای: xenorhabdus poinarii
تعداد نتایج: 383 فیلتر نتایج به سال:
Characterization and environmental regulation of outer membrane proteins in Xenorhabdus nematophilus
During the search for novel natural products from entomopathogenic Xenorhabdus doucetiae DSM17909 and X. mauleonii DSM17908 novel peptides named xenoamicins were identified in addition to the already known antibiotics xenocoumacin and xenorhabdin. Xenoamicins are acylated tridecadepsipeptides consisting of mainly hydrophobic amino acids. The main derivative xenoamicin A (1) was isolated from X....
Xenorhabdus nematophila is an insect pathogen and produces protein toxins which kill the larval host. Previously, we characterized an orally toxic, large, outer membrane-associated protein complex from the culture medium of X. nematophila. Here, we describe the cloning, expression, and characterization of a 17-kDa pilin subunit of X. nematophila isolated from that protein complex. The gene was ...
This study was carried out to determine the antifungal effects of supernatant produced by bacterium Xenorhabdus szentirmaii, which is associated with soil-inhabiting entomopathogenic nematodes, on important plant pathogenic fungi, Fusarium verticilliodes, oxysporum f.sp lycopersici, radicis Botrytis cinerea, Sclerotinia sclerotiorum and Phytophthora nicotianae. The 1, 3, 5 7% concentrations X. ...
Photorhabdus and Xenorhabdus are the bacterial symbionts of insect pathogenic nematodes, Heterorhabditis Steinernema, respectively. This study aims to characterize from Mizoram, North-east India evaluate their antibacterial potential. The isolates were characterized using recA gyrB gene regions. ethyl acetate extract was tested against strains, viz. Escherichia coli (ATCC 10536), Klebsiella pne...
Bacterial toxin-antitoxin (TA) complexes induce programmed cell death and also function to relieve cell from stress by various response mechanisms. Escherichia coli RelB-RelE TA complex consists of a RelE toxin functionally counteracted by RelB antitoxin. In the present study, a novel homolog of RelE toxin designated as Xn-relE toxin from Xenorhabdus nematophila possessing its own antitoxin des...
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