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  • 1
    ISSN: 1573-0832
    Keywords: Candida albicans ; Cell wall ; Germ tube ; Monoclonal antibody ; Surface antigen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Monoclonal antibodies against germ-tube specific antigens ofCandida albicans were produced by a selective immunization protocol. The monoclonal antibody (MAb) DC3:H10 recognized a determinant preferentially expressed by germ tubes of the fungus compared to yeast cells. The MAb DC3:H10 antigen was expressed by nearly all germ tubes of the strains 3153A and B311. It was also expressed by germ tubes of the white phenotype of strain WO-1, and by many exponentially growing yeast cells of the opaque phenotype of this strain. The determinant appeared very rapidly after induction of germ tubes of strain 3153A. The MAb DC3:H10 epitope was sensitive to proteolytic treatment but not to periodate treatment, indicating its protein nature. The reactive material could be extracted from intact germ tubes by treatment with β-mercaptoethanol. On elution from a G-200 Sephadex column it yielded an apparent molecular weight of 519 kDa. This fraction appeared heterogeneous since at least two major bands of lower molecular weight were detected by silver staining following electrophoretic separation under denaturing conditions.
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  • 2
    ISSN: 1573-0832
    Keywords: Candida albicans ; Cell wall ; Complexes ; Mannoproteins ; Receptors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have previously described a monoclonal antibody, MAb DC3:H10, which recognized an epitope preferentially expressed on the surface ofCandida albicans germ tubes. In the present study we examined the MAb-reactive material further. Immunoblot analysis of the material purified partially by Sephadex G-200 and DEAE-Sephacel chromatography reacted with antibodies to theC. albicans C3d receptor (CR2). In an ELISA, MAb DC3:H10 captured antigen that was recognized by both anti-CR2 and anti-mp58 fibrinogen binding mannoprotein polyclonal antibodies. The MAb DC3:H10 failed to compete with either of these antisera in an ELISA. Indirect immunofluo-rescence (IIF) analysis showed differences in surface distribution for the MAb DC3:H10, the CR2, and the mp 58 epitopes. Dual labeling IIF experiments showed MAb DC3:H10 binding to be unaffected by binding of fibrinogen or anti-mp58 antibody. However, the binding patterns of MAb DC3:H10 were modified in the presence of anti-CR2 antibody, suggesting a complex interaction between these cell wall components.
    Type of Medium: Electronic Resource
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