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  • 1
    ISSN: 1432-072X
    Keywords: Candida albicans ; Cell growth ; Budding ; Mycelium ; Cell wall ; Mannoproteins ; Concanavalin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Depending upon growth temperature, Candida albicans can exhibit two different morphologies, a budding yeast or a mycelium. By studying the distribution of concanavalin A-ferritin particles on the cell wall surface during bud and germ tube formation, we have elucidated the way cell wall extension occurs. Both processes initially require the localized lysis of the wall in order to allow the incorporation of the newly synthesized material. Later on, the cell wall behaves as an elastic structure, allowing extension by an intosusception process and, as a consequence, cell growth.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Candida albicans ; Mannoproteins ; Tunicamycin ; Concanavalin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The kinectics of incorporation of two precursor mannoproteins into the regenerating cell wall of Candida albicans protoplasts have been followed at 28°C and 37°C using two monoclonal antibodies specific for protein epitopes (MAb 1B12 and 4C12) as probes. Both molecules were secreted from the beginning of the regeneration process, and their incorporation was retarded significantly. Analysis of the secreted materials by Western immunoblotting with MAb 1B12 allowed the identification of two closely migrating bands at apparent Mr higher than 170 kDa and significant amounts of a highly polydisperse material of even greater molecular mass. Some of these mannoproteinaceous species carried both N- and O-glycosidically linked mannose residues, as deduced from their drop in apparent Mr when synthesized in the presence of tunicamycin and by their reactivity with Concanavalin A. Following secretion, the molecules reacting with MAb 1B12 were incorporated into the regenerating walls by covalent binding. Then, when the regenerating walls by covalent binding. Then, when the antigen molecules were solubilized from partially regenerated walls, their mobility differed when regeneration took place at 28°C (blastoconidia) or 37°C (mycelial cells).
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 132 (1982), S. 144-148 
    ISSN: 1432-072X
    Keywords: Yeast ; Cell wall ; Mannoproteins ; Envelope turnover ; Concanavalin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By pulse and chase labeling experiments, two independent mannoprotein pools have been found associated with the Saccharomyces cerevisiae envelope. One of them probably corresponds to mannoproteins localized in the periplasmic space. These molecules showed a high turnover rate at 28° C. The second pool is formed by intrinsic wall mannoproteins which are apparently stable for long periods of time, after a small initial turnover. These results suggest that at least part of the mannoproteins initially found in the periplasmic space may move into the wall. The time lag between the addition of the radioactive precursors and their incorporation in the cell envelope (20–30 min for amino acids and about 10 min for carbohydrate) indicates that protein formation and carbohydrate incorporation take place in succession. Moreover, bulk glycosylation of mannoproteins seems to occur close in time to the moment of secretion into the periplasmic space.
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