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  • 1
    Electronic Resource
    Electronic Resource
    Potential for using host resistance to reduce production of pseudothecia and ascospores of Leptosphaeria maculans, the blackleg pathogen of Brassica napus (2004)
    Oxford, UK : Blackwell Science Ltd
    Plant pathology 53 (2004), S. 0 
    Details
    ISSN: 1365-3059
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Pseudothecial density of the blackleg fungus Leptosphaeria maculans and discharge of ascospores was measured from stubble of a range of Brassica species, including Brassica napus (canola) cultivars, with a range of blackleg resistance. Since ascospores are the primary inoculum, these parameters reflect inoculum potential for blackleg. Stubble from a representative line of each of B. carinata, B. nigra, Sinapis alba and B. napus cv. Surpass 400 (incorporates blackleg resistance from B. rapa ssp. sylvestris) had lower pseudothecial density and discharged fewer ascospores than stubble of other B. napus cultivars (Karoo, Oscar, Emblem, Dunkeld and Columbus). These latter B. napus cultivars and a representative B. juncea line had higher pseudothecial densities and discharged higher numbers of ascospores. If this trait of low blackleg inoculum from stubble could be introgressed into commercial canola cultivars, blackleg disease severity could be substantially reduced, resulting in higher and more stable canola yields. However, the trait of reduced ascospore discharge may not be stable, as demonstrated by the B. rapa ssp. sylvestris-derived resistance already being overcome by the blackleg fungus in Australia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3059.2004.01050.x
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  • 2
    Electronic Resource
    Electronic Resource
    Cross-reactivity between Acacia (wattle) and rye grass pollen allergens (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical & experimental allergy 12 (1982), S. 0 
    Details
    ISSN: 1365-2222
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Immunoglobulin E (IgE), directed against components of Acacia (wattle) pollen, has been detected by radioallergosorbent tests (RAST) in the sera of some children and adults who develop allergic symptoms in the presence of flowering Acacia trees in Australia. All these subjects also had high levels of IgE directed against Lolium perenne (rye grass) pollen. Inhibition by RAST showed that most of the IgE molecules which bound to Acacia pollen components also bound to L. perenne pollen extracts, and to Glycoprotein I, the major allergen of L. perenne pollen. In these assays, the allergens have been immobilized on polyvinyl chloride microtitre trays: the sensitivity of this approach is compared to that of commercial RAST kits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2222.1982.tb02526.x
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  • 3
    Electronic Resource
    Electronic Resource
    Characterisation of a cyanide hydratase gene in the phytopathogenic fungus Leptosphaeria maculans (2000)
    Springer
    Molecular genetics and genomics 263 (2000), S. 463-470 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsLeptosphaeria maculans ; Cyanide hydratase ; Brassica ; Glucosinolate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A gene encoding a cyanide hydratase was cloned from an aggressive isolate of Leptosphaeria maculans, the fungus which causes blackleg disease of oilseed Brassica spp. This enzyme catalyses the breakdown of hydrogen cyanide to a less toxic compound, formamide. The predicted amino acid sequence of cyanide hydratase in L. maculans is 77% and 82% identical to cyanide hydratases from two other ascomycetes, Gloeocercospora sorghi and Fusarium lateritium, respectively. The gene is present as a single copy in the L. maculans genome, in both aggressive and non-aggressive isolates, although there is a restriction fragment length polymorphism between these two isolate groups for this gene. The cyanide hydratase promoter contains four putative target sites for GATA transcription factors, proteins that regulate nitrogen metabolism and other processes. Transcription of cyanide hydratase in an aggressive L. maculans isolate is induced strongly by potassium cyanide. Transcription of the gene is detectable in cotyledons of Brassica juncea and B. napus during infection. L. maculans can utilise the reaction product, formamide, as a sole source of nitrogen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051190
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  • 4
    Electronic Resource
    Electronic Resource
    Botanical immunocytochemistry: a review with special reference to pollen antigens and allergens (1980)
    Springer
    Journal of molecular histology 12 (1980), S. 247-272 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01006951
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Immunofluorescent localization of two water-soluble glycoproteins including the major allergen from the pollen of ryegrass,Lolium perenne (1981)
    Springer
    Journal of molecular histology 13 (1981), S. 461-480 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Two major glycoproteins have been localized in sectioned grains of ryegrass pollen by direct and indirect immunofluorescence methods using Fluorescein isothiocyanate (FITC)-labelled IgC fractions of antisera. These glycoproteins are the major allergen Group 1 allergen, and a principal antigen Antigen A. Four methods of fixation were employed: freeze-drying, methanol, 2.5% glutaraldehyde and 4% paraformaldehyde for 1 h at 4°C. The post-embedding staining technique of immunocytochemistry was used: anthers were embedded directly, or after dehydration, in JB-4 plastic resin and antibody reacted with sectioned pollen. The effects of these fixatives on the antibody combining sites of the antigens were quantified by a solid phase radioimmunoassay using [125I]protein A to measure antibody binding. Glutaraldehyde was the only fixative to significantly depress antibody binding of both Antigen A and Group 1 allergen to their homologous antisera. This radioimmunoassay was modified to reyeal that FITC conjugation to either antibody did not impair antigen binding. In mature pollen, these antigens were located in the cytoplasm and in the complex wall. In developing grains early in the maturation period, specific fluorescence was concentrated at the periphery of the cytoplasm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01005062
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of water-soluble glycoproteins, including Group 1 allergen, in pollen of ryegrass,Lolium perenne, using ferritin-labelled antibody (1982)
    Springer
    Journal of molecular histology 14 (1982), S. 949-966 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The cellular sites of the glycoproteins Group 1 allergen (glycoprotein 1) and Antigen A (glycoprotein 2) in mature ryegrass pollen have been investigated by immunoelectron microscopy. Radioimmunoassays confirm previous findings of cross-reactivity between the purified glycoprotein antigens at the high immunoglobulin G (IgG) concentrations used for localization. Freeze-drying of anthers followed by anhydrous processing has been employed because of the water solubility and mobility of the glycoproteins. A double-embedding technique has been developed. This involves, first, embedding anthers in the water-soluble plastic resin JB-4, sectioning and incubating in ferritin-labelled antisera by the indirect method. The sections are then embedded in Spurr's resin for ultra-thin sectioning. Both glycoproteins are found in the following sites: (1) exine and intine wall layers; (2) pollen cytoplasm; (3) the orbicules and anther loculus; and (4) the anther cuticle. In the exine arcades and surface and in the anther loculus, the ferritin label is bound to pollenkitt. The finding that the glycoproteins are in similar sites is predictable in view of the cross-specificity of the antisera. The extent of antibody penetration of the plastic sections has been examined; labelling is confined to cut grains and absent from intact grains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01005236
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