Disease relevance of Verticillium

• Plant susceptibility to five of the eight pathogens we examined was reduced by the jasmonate response, including two bacteria (Pseudomonas syringae and Xanthomonas campestris), two fungi (Verticillium dahliae and Fusarium oxysporum f. sp. lycopersici), and an oomycete (Phytophthora infestans) [1].

High impact information on Verticillium

• Gossypol levels were not reduced in the seeds of transformants with either construct, nor was the induction of CDNS expression affected in stems of the constitutive antisense plants infected with Verticillium dahliae Kleb [2].
• Unique diketopiperazine dimers from the insect pathogenic fungus Verticillium hemipterigenum BCC 1449 [3].
• Nearly 100% 5'-position selectivity of transglucosylation from maltodextrin to pyridoxine (PN) by cells of Verticillium dahliae TPU 4900 was observed when the reaction was carried out with borate [4].
• Cloning of two contrasting high-affinity sulfate transporters from tomato induced by low sulfate and infection by the vascular pathogen Verticillium dahliae [5].
• The 331 Verticillium antagonists were identified by their fatty acid methyl ester profiles [6].

Biological context of Verticillium

• In vitro analysis of the role of glucose oxidase from Talaromyces flavus in biocontrol of the plant pathogen Verticillium dahliae [7].
• The antifungal activity against the major pathogens responsible for important plant diseases (Botrytis cinerea, Myrothecium and Verticillium dahliae dleb) of N-(piperidylthiocarbonyl) benzamide and its complex with cobalt (III) are studied and compared with N-(morpholinothiocarbonyl) benzamide [8].
• Sixteen isolates of different pathogenicity groups of the plant pathogen Verticillium dahliae and four isolates of V. albo-atrum from Japan were analysed by means of an RAPD (random amplified polymorphic DNA) method using a PCR (polymerase chain reaction) [9].
• Sharing high homologies to tomato verticillium wilt disease resistance genes Ve1 and Ve2, SlVe1 encoded a cell-surface glycoprotein with receptor-mediated endocytosis-like signal [10].

Anatomical context of Verticillium

• 0. The optimum temperature for the two chitinase activities was 40 degrees C. The two chitinases had activity against cell wall of Verticillium dahliae, Sclerotinia sclerotiorum and Rhizoctonia solani, and inhibited spore germination and germ tube elongation of Alternaria alternata, Fusarium moniliforme, and Magnaporthe grisea [11].

Associations of Verticillium with chemical compounds

• Treatment of lucerne suspension culture cells with glycoprotein elicitor from the phytopathogenic fungus Verticillium albo-atrum R & B triggers Ca(2+)-mediated induction of antimicrobial secondary metabolites termed phytoalexins [12].
• Differential induction of 3-hydroxy-3-methylglutaryl CoA reductase in two cotton species following inoculation with Verticillium [13].
• One of these metabolites, scytalone, was racemic and thus different than the (+)-enantiomer from Verticillium dahliae [14].
• Optimization of the chiral inversion of 2-phenylpropionic acid by Verticillium lecanii [15].
• Ultrastructural changes and location of beta-1, 3-glucanase in resistant and susceptible cotton callus cells in response to treatment with toxin of Verticillium dahliae and salicylic acid [16].

Gene context of Verticillium

• Expression and regulation of casein kinase 2 during heat shock in Verticillium dahliae [17].
• Phylogenetic relationships among 18 isolates in the genus Verticillium, representing 13 species of diverse econutritional groups (pathogens of insects, plants, mushrooms, nematodes and spiders, and saprobes), were examined by using sequences from the internal transcribed spacer (ITS) and small nuclear (NS) rRNA regions [18].
• ES-242-2, -3, -4, -5, -6, -7, and -8, novel bioxanthracenes produced by Verticillium sp., which act on the N-methyl-D-aspartate receptor [19].
• A polymerase chain reaction-based test for Verticillium fungicola causing dry bubble disease on the cultivated mushroom, Agaricus bisporus [20].
• Production of an extracellular trypsin-like protease by the fungal plant pathogen Verticillium dahliae [21].

References