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  • 1
    ISSN: 1615-6102
    Keywords: Adhesion ; Carbohydrates ; Exocytosis ; K-bodies ; Lectins ; Saprolegnia ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Electron and fluorescence microscopy were used to identify organelles involved in attachment of secondary zoospores ofSaprolegnia ferax as they were transformed into secondary cysts. When secondary zoospores were exposed to 1.0% peptone in the absence or presence of a substrate, they began to encyst. If substrates were present when encystment was induced, the groove surface of the secondary zoospores adhered to them. The first event in attachment was secretion of contents of the kinetosome-associated organelle (K-body), which was typically oriented with the tubule-filled cavity positioned toward the cell surface of the groove region in the zoospore. The tubules which contained carbohydrates became coarsely granular, the matrix became more fibrous, and the shell remained along the membrane concavity that was formed as the K-body fused with the plasma membrane. Five minutes later, a cyst coat appeared, and cysts were not readily dislodged from a substrate. The concavity was no longer found, presumably because it had evaginated; but a layered pad of adhesion material was between the cyst coat and substrate. The layers of the adhesion pad corresponded to the structure of the matrix of K-bodies. As with the tubules of the K-body, the coarsely granular portion at the edge of the pad stained for carbohydrates. Similarly, the lectins WGA and GS-II labeled with fluorescein stained the rim of the adhesion pad on cysts, indicating the presence of glycoconjugates containing N-acetylglucosamines. Because globular areas near the kinetosomes and groove of zoospores (where K-bodies were located) also bound WGA and GS-II, K-bodies contained the same carbohydrates as the adhesion pad. We conclude that K-bodies function in the attachment of encysting zoospores to substrates as the cell differentiates. The tubular portion of the K-body matrix contains carbohydrates which might assist in the adhesion process.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1615-6102
    Keywords: Plectonema boryanum ; Cyanobacteria ; Ultrastructure ; Nitrogen fixation ; Nitrogen starvation ; Immunogold localization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ultrastructure of fructose-supplemented and unsupplemented nitrogen-fixing (fix +) and nonfixing (fix −)Plectonema boryanum UTEX 581 cells was examined by transmission electron microscopy. The most prominent structural differences included the arrangement and morphology of the thylakoids and alterations in the appearance of the interthylakoidal spaces. These ultrastructural differences, together with other observations such as glycogen content and presence of nitrogenase (using acetylene reduction assay and immunogold localization), readily distinguished nonfixingP. boryanum from nitrogen-fixing cells.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 175 (1993), S. 161-172 
    ISSN: 1615-6102
    Keywords: Carbohydrates ; Cell surface ; Lectins ; Oomycetes ; Saprolegnia ; Spores
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In asexual reproduction of the water mold,Saprolegnia ferax, four distinct and sequentially produced spores are involved in dispersal, two of which are motile and two of which are nonmotile. Composition of cell surface glycoproteins may be important in dispersal strategies for each of these stages. Binding patterns of fluorescently labelled lectins were investigated to identify differences in glycoproteins of asexually produced dispersal stages. The pattern of lectin binding to zoospores was diverse. FITC-Con A bound to surfaces of zoospores and membranes of the water expulsion vacuole system, indicating the prescence of mannosyl and glucosyl residues. In zoospores incubated for more than 30 min in FITC-WGA and FITC-GS II. which bind N-acetyl glucosamine, fluorescence was sometimes localized in peripheral, intracellular patches. In shorter incubations, secondary zoospores bound these lectins along the groove region where K-bodies were located. Surfaces of cystospores typically bound FITC-WGA, but not FITC-GS II. FITC-GS II, however, bound to empty cystospore walls, probably because reactive sugars were available at the inner surface of the wall. Germ tubes emerging from cystospores bound labelled WGA and GS II, but not Con A. The same lectin binding pattern was found along discharge papilla of primary cystospores, indicating that modifications in cystospore walls associated with direct germination and zoospore discharge were similar. Thus, glycoproteins involved in early establishment of the hyphal system differ from those forming the cell surface of cystospores. Differences in the binding pattern of lectins to zoospores and cystospores highlight differences between cell surface carbohydrates of motile and nonmotile asexual stages.
    Type of Medium: Electronic Resource
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