Immunoblotting analysis of sera from patients with candidal vaginitis and healthy females

Ishiguro, Akira; Homma, Michio; Sukai, T.; Higashide, K.; Torii, S; Tanaka, Kenji

doi:10.1080/02681219280000371

Cited by 15 publications

(15 citation statements)

References 20 publications

(16 reference statements)

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“…Tlie IgG4 detection showed reactivity in the high MW zone corresponding to C. albicans mannan. This is in accordance with previously published data (29) indicating that a short-term sensitizing antibody, probably IgG4, was elicited by mannans. It appeared that a vast array of C. albicans antigens elicits IgG3 production, but not production of the other subclasses, where reactive bands were fewer.…”

Section: Discussionsupporting

confidence: 94%

“…Shen et al (28) have identified a 40-kDa major allergen of C. albicans among asthmatic patients as an alcohol dehydrogenase. Ishiguro et al (29) identified various C. albicans allergens and purified three components (37, 43, and 46 kDa) from eytoplasmic fractions of C. albicans extract. Those tliree components appeared to be homologous to S. cerevisiae aldolase, phosphoglycerate kinase, and enolase, respectively The protein allergen described by Savolainen et al (25) had a MW of 46 kDa but represented a major allergen only in a pediatric asthmatic population.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Anti‐Candida albicans IgE and IgG subclasses in sera of patients with allergic bronchopulmonary aspergillosis (ABPA)

Roig

Malo

Montplaisir

1997

Allergy

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We performed immunoblotting experiments to determine specific IgE and IgG subclass responses to Candida albicans antigens in allergic bronchopulmonary aspergillosis (ABPA) patients. This is a first report describing C. albicans antigens recognized by serum IgE and IgG subclasses of ABPA patients sensitized to that yeast. Among the various antigens reacting with serum IgE, a 43-kDa component was recognized by all seven patients and can be considered a major antigen of C. albicans for this particular group of patients. By comparison, only 20% of a group of asthmatic atopics (25 patients) and 10% of a group of normal controls (10 subjects) were 43-kDa positive. Multiple banding patterns, revealing no major antigen, were observed for all four IgG subclasses except for IgG1 in one case. In particular, the 43-kDa component was not always recognized by all the patients. Furthermore, oral or inhaled steroid treatment appears to have no impact on the specific IgE immunopatterns obtained. Using immunoelectron-microscopy, we localized IgE-binding primarily in the mannoprotein-containing layers of the C. albicans cell wall. In conclusion, C. albicans-IgE and IgG subclasses may participate in the physiopathology of ABPA by exacerbating pulmonary infiltrates (IgE) and inducing eosinophil-mediated inflammatory reaction (IgG1, IgG3).

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Section: Discussionsupporting

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Anti‐Candida albicans IgE and IgG subclasses in sera of patients with allergic bronchopulmonary aspergillosis (ABPA)

Roig

Malo

Montplaisir

1997

Allergy

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“…3; number 15) were identified as PGK. This glycolytic enzyme has previously been characterised as an antigen that reacts with IgE antibodies present in sera from allergic patients [21].…”

Section: By Immunoblot Analysismentioning

confidence: 99%

“…Spot 19 showed homology to a C. albicans antigen that is reactive with an IgE antibody of sera from allergic patients [21]. This IgE-binding antigen is the glycolytic enzyme [8,9].…”

Section: Protein Identification By N-terminal Sequence Analysismentioning

confidence: 99%

Analysis of the serologic response to systemicCandida albicans infection in a murine model

et al. 2001

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Two different strains of mice with different susceptibilities to systemic candidiasis (BALB/c and CBA/H) were infected with Candida albicans SC5314. Immune sera were obtained on different days post-infection and assayed against two-dimensional polyacrylamide gel electrophoresis separation of cytoplasmic extracts obtained from protoplasts. More than 31 immunoreactive proteins were detected. Some of them were identified and found to correspond to (i) glycolytic enzymes, such as fructose biphosphate aldolase, triose phosphate isomerase (TPIS), glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase (PGK), enolase (ENO1) and pyruvate kinase, (ii) other metabolic enzymes, such as methionine synthase (METE), inosine-5'-monophosphate dehydrogenase (IMH3), alcohol dehydrogenase and aconitate hydratase and (iii) heat shock proteins: HS71 (or Ssa1p) and HS75 (or Ssb1p), both from the HSP70 family. This work reports for the first time antigenic properties for IMH3 and TPIS. Different profiles of antibody expression, depending on the mouse strain and the course of infection, were observed. ENO1 was the most immunogenic protein in infected BALB/c mice (the most resistant strain). On the other hand, sera from CBA/H mice (a more susceptible strain) showed a strong increase in reactivity along the infection against METE, HS75 and PGK. Many of these immunoreactive proteins have also been detected using sera from human patients with systemic candidiasis, thus indicating the usefulness of the murine model for studying the antibody response in systemic candidiasis. In this work we demonstrate that the combination of two-dimensional electrophoresis with immunoblotting using murine immune sera can be an important tool for the identification of C. albicans antigens and for monitoring the evolution of the disease.

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“…The identification of glycolytic enzymes as immunogens during candidiasis is well documented. Thus, C. albicans enolase, phosphoglycerate kinase, alcohol dehydrogenase, pyruvate kinase, and aldolase have been described as major allergens/immunogens during candidiasis [7–16]. In addition, the presence of glycolytic enzymes on C. albicans cell wall is not unprecedented.…”

Section: Introductionmentioning

confidence: 99%

Clinical strains ofCandida albicansexpress the surface antigen glyceraldehyde 3-phosphate dehydrogenase in vitro and in infected tissues

Gil

Villamón

Monteagudo

et al. 1999

FEMS Immunology &Amp; Medical Microbiology

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We have previously described the presence of an enzymatically active form of glyceraldehyde 3-phosphate-dehydrogenase (GAPDH) in the cell surface of Candida albicans ATCC 26555 which is also a fibronectin and laminin binding protein. Immunohistochemical analysis of tissue sections from patients with disseminated candidiasis with a polyclonal antiserum to GAPDH from C. albicans (PAb anti-CA-GAPDH) revealed that the enzyme is expressed at the surface of fungal cells in infected tissues. The same PAb detected the presence of GAPDH species, with a molecular mass of approximately 33 kDa, in cell wall extracts obtained from clinical isolates of the fungus. These cell surface-bound GAPDH moieties exhibited a dose-dependent dehydrogenase activity. These results indicate that this cell surface-bound GAPDH plays a role during infection probably contributing to the attachment of fungal cells to host tissues.

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Immunoblotting analysis of sera from patients with candidal vaginitis and healthy females

Cited by 15 publications

References 20 publications

Anti‐Candida albicans IgE and IgG subclasses in sera of patients with allergic bronchopulmonary aspergillosis (ABPA)

Anti‐Candida albicans IgE and IgG subclasses in sera of patients with allergic bronchopulmonary aspergillosis (ABPA)

Analysis of the serologic response to systemicCandida albicans infection in a murine model

Clinical strains ofCandida albicansexpress the surface antigen glyceraldehyde 3-phosphate dehydrogenase in vitro and in infected tissues

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