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  • Plant disease  (2)
  • Basidiomycete  (1)
  • Springer  (3)
  • Institute of Physics
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  • Springer  (3)
  • Institute of Physics
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 181 (1994), S. 202-212 
    ISSN: 1615-6102
    Keywords: Fungal adhesion ; Appressoria ; Plant disease ; Cochliobolus heterostrophus ; Magnaporthe grisea ; Nectria haematococca ; Uromyces spp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Firm adhesion of fungal plant pathogens to their hosts is critical at several stages in the host-parasite interaction. Spores of many fungal species are capable of rapid, non-specific attachment to various surfaces. This early adhesion, which often occurs well before germ tube emergence, prevents spores from being blown or washed from the host surface before infection can take place. Adhesion is critical for proper sensing of topographic signals involved in thigmotropic responses and for differentiation and function of appressoria. Four fungal pathogens which exhibit a variety of adhesion mechanisms have been selected for discussion.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 103 (1980), S. 281-297 
    ISSN: 1615-6102
    Keywords: Basidiomycete ; Fixation technique ; Freeze-substitution ; Fungi ; Laetisaria arvalis ; Ultrastructure preservation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ultrastructure of freeze-substituted (FS) hyphae ofLaetisaria arvalis is described and compared to that of similar hyphae preserved by conventional chemical fixation (CF). The outline of membrane-bound organelles as well as the plasma membrane was smooth in FS cells. In contrast, hyphae preserved by CF exhibited membrane profiles that were extremely irregular. Centers of presumed Golgi activity were best preserved by FS. Microvesicles, 27–45 nm diameter and hexagonal in transverse section, were observed most readily in FS cells. Filasomes (= microvesicles within a filamentous matrix) were only observed in FS cells. Apical vesicles, 70–120 nm diameter, associated with the centers of Golgi activity and within the Spitzenkörper region exhibited finely granular matrices in FS hyphae, whereas in CF hyphae the contents were coarsely fibrous and less electron-dense. Microvesicles were present at hyphal apices and regions of septa formation. Filasomes were also found at regions of septa formation as well as along lateral hyphal tip cell walls. Microvesicles, but not filasomes, were observed in membrane-bound vesicles (= multivesicular bodies) and in larger vacuoles. Filaments, 5.2–5.4 nm wide, were juxtaposed with centripetally developing septa. Cytoplasmic inclusions, 20–40 μm in length, composed of bundles of 6.7–8.0 nm wide filaments were observed in both FS and CF hyphae.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 168 (1992), S. 20-26 
    ISSN: 1615-6102
    Keywords: Appressoria ; Freeze substitution ; Immunofluorescence ; Plant disease ; Phalloidin ; Pyricularia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The penetration peg is the structure used byMagnaporthe grisea to pierce the surface of rice leaves or very hard nonbiodegradable substrates. Penetration pegs produced by appressoria in vitro were examined by electron microscopy and immunofluorescence microscopy using various fluorophore labeled anti-actins. Freeze-substitution preparation of appressoria at early stages of substrate penetration showed that peg cytoplasm consisted primarily of a zone of exclusion, excluding even ribosomes, and was continuous with a similar region in the appressorium. Apical vesicles were, however, observed in short, presumably elongating pegs. Immunofluorescence microscopy was used to demonstrate binding of a monoclonal anti-actin to penetration peg cytoplasm, following “permeabilization” of appressoria by means of a brief sonication. Occasional filaments and ca. 300 nm diameter plaques were labeled in appressorial cytoplasm. Western blot analysis of germ tube extracts showed that the monoclonal probe bound predominantly to a single band with a molecular weight similar to that of rabbit muscle actin. Preincubation of the antibody with actin virtually eliminated peg labeling. We conclude that the penetration peg contains actin which may play a role in the formation of the zone of exclusion.
    Type of Medium: Electronic Resource
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