Isolation of immunodominant antigens from sera of patients with systemic candidiasis and characterization of serological response to Candida albicans

Matthews, Ruth; Burnie, James; Tabaqchali, Soad

doi:10.1128/jcm.25.2.230-237.1987

Cited by 160 publications

(67 citation statements)

References 17 publications

(23 reference statements)

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“…The significance of the 40 kD major allergen in C alhicans is unclear. In disseminated candidiasis, antibodies to the 40 kD antigen could be detected in about 20% ofthe patients [18] although the 47 kD component seems to be the predominant antigen [18][19][20]. However, one cannot be certain ofthe consistency ofthe assignment of MW to the observed antigens in different laboratories without direct comparison.…”

Section: Discussionmentioning

confidence: 98%

Allergenic components of Candida albicans identified by immunoblot analysis

Shen

Choo

Tang

et al. 1989

Clin Experimental Allergy

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Allergenic components of Candida albicans fractionated by SDS-polyacrylamide gel electrophoresis (PAGE) and transferred to nitrocellulose membranes were identified using sera from 30 asthmatic patients who showed positive skin test and RAST (radio-allergosorbent test) to C. albicans. The IgE-binding yeast components in the complex antigen preparation were then detected by reaction with enzyme-labelled anti-human IgE antibodies. They were confirmed by Coomassie blue R-250 staining of the membrane to visualize all protein bands after reaction with the enzyme substrate. The IgE-binding patterns of the sera tested were heterogeneous, displaying a total of 16 identifiable components with molecular weights ranging from 20 to 94 kD. A 40 kD component showed the highest IgE-binding frequency, being recognized by 23 (77%) of the 30 sera examined. The other 15 allergenic components identified were recognized by less than 25% of the sera tested. Only two of the 30 serum samples contained IgE antibodies reactive with seven to eight allergenic components. Ten of the 30 sera reacted with only one allergenic component, and the remaining serum samples recognized two to five of the 16 identified allergens. Results described in this study are applicable to allergen standardization work and provide a basis for further study on the role of C. albicans in clinical allergy.

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Section: Discussionmentioning

confidence: 98%

Allergenic components of Candida albicans identified by immunoblot analysis

Shen

Choo

Tang

et al. 1989

Clin Experimental Allergy

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“…Antibodies to various Candida antigenic determinants were regularly found in CMC patients, often in high titre [12]. Several studies have emphasized the importance of anti-Candida antibodies in protection from systemic candidiasis, and in fact CMC patients rarely if ever develop systemic disease [13]. Only recently has it been shown that patients with CMC are susceptible to non-Candida infections as well, especially those caused by encapsulated bacteria, where protection is mediated by antibodies directed toward bacterial polysaccharide components [5].…”

Section: Discussionmentioning

confidence: 99%

Chronic mucocutaneous candidiasis. II. Class and subclass of specific antibody responses in vivo and in vitro

Lilić¹,

Calvert²,

Cant

et al. 1996

Clinical and Experimental Immunology

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SUMMARYPatients with chronic mucocutaneous candidiasis (CMC) succumb to persistent infections with the opportunistic yeast Candida. Impaired cell-mediated responses to Candida have been repeatedly reported while antibody responses were mostly found to be normal. The underlying defect remains poorly understood. It has recently been shown that CMC patients are also susceptible to infections with encapsulated bacteria, and may have associated IgG2 and IgG4 deficiency. Our previous studies demonstrated altered cytokine production in CMC patients. As cytokines can influence production and isotype of specific antibody, in 10 patients with CMC we measured the levels and isotype distributions of serum antibodies to Candida antigens (CAg), pneumococcal polysaccharide (PPS) and tetanus toxoid (TT) antigens. Peripheral blood lymphocytes were also stimulated in culture and the antibodies made in vitro were measured. Our data demonstrated that in vivo, CMC patients had very high levels of IgG and IgA CAg-specific antibodies. CAg-specific and PPS-specific IgG1 was markedly higher than in controls. Children but not adults with CMC had significantly lower levels of IgG2-specific antibody to CAg and PPS compared with age-matched controls. Patients had significantly higher levels of IgG3-specific antibody to all three antigens tested. These findings were in accordance with increased total IgG and IgG3 levels seen in CMC patients. In vitro, CMC patients, particularly children, did not respond as frequently to antigen stimulation as did their healthy controls. The level of specific antibody produced was also lower to all antigens tested, as was the amount of total immunoglobulins following antigenic and particularly mitogenic stimulation. Addition of interferon-alpha (IFN-®) or IFN-°to cultures had variable, sometimes marked, effects. Our results demonstrate that CMC patients manifest subtle alterations in specific antibody responses to CAg, PPS and TT, which are most pronounced in children. This may relate to altered cytokine production also seen in these patients.

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“…The 44-kDa band does not demonstrate the heat-inducibility of the 68-kDa band and may represent an accumulated degradation fragment of the intact protein due to autolytic or degradative pathways described for other stress protein families [13]. This ¢nding is also reminiscent of studies by Matthews et al [14], who described a predominant 47-kDa fragment of the C. albicans Hsp90 protein.…”

Section: Discussionmentioning

confidence: 58%

Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis

Lopatin

1999

FEMS Microbiology Letters

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We previously reported an association between elevated serum antibody titers to the 90-kDa human heat shock protein (Hsp90), periodontal health and colonization by Porphyromonas gingivalis. In this study, we examined the cellular localization of the Hsp90 homologue of P. gingivalis. Cultures of P. gingivalis were heat-stressed (45³C) and examined for localization of the Hsp90 homologue. Heat stress induced a 4^5-fold increase in anti-Hsp90 antibody reactivity over that of the unstressed controls. Western blot analysis revealed two bands (44 and 68 kDa) that reacted with anti-Hsp90 antibodies. The 68-kDa band was heat-inducible, while the 44-kDa band was not. Immunogold staining revealed that the Hsp90 homologue localized principally to the membrane and extracellular vesicles. Subcellular fractionation confirmed that the Hsp90 homologue was primarily membrane-associated. ß 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. Keywords : Heat shock; Extracellular vesicle ; 90-kDa human heat shock protein; Porphyromonas gingivalis 0378-1097 / 99 / $20.00 ß 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. PII: S 0 3 7 8 -1 0 9 7 ( 9 9 ) 0 0 5 0 6 -6 * Corresponding author. Tel.: +1 (734) 647-3912; Fax: +1 (734) 764-2425.FEMS Microbiology Letters 181 (1999) 9^16

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Isolation of immunodominant antigens from sera of patients with systemic candidiasis and characterization of serological response to Candida albicans

Cited by 160 publications

References 17 publications

Allergenic components of Candida albicans identified by immunoblot analysis

Allergenic components of Candida albicans identified by immunoblot analysis

Chronic mucocutaneous candidiasis. II. Class and subclass of specific antibody responses in vivo and in vitro

Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis

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