Probable presence of beta(1-2)-linked oligomannosides that act as human immunoglobulin G3 epitopes and are distributed over a Candida albicans 14- to 18-kilodalton antigen

Poulain, D.; Faille, Christine; Delaunoy, C; Jacquinot, Pierre Marie; Trinel, Pierre-André; Camus, Daniel

doi:10.1128/iai.61.3.1164-1166.1993

Cited by 18 publications

(15 citation statements)

References 9 publications

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“…This suggests the presence of discriminating epitopes in both the alkali-stable and the alkalilabile domains of the PPM polysaccharide moiety. Specificity of antioligosaccharide antibodies depends on the mannosyl chain length (9), the anomeric configuration (10,29,34,39,42), and the position of linkage (17). Thus it could be speculated that, within the oligomannosidic repertoire of this strain, the best candidate for an epitope discriminating between CD and UC is the mannotetraose.…”

Section: Discussionmentioning

confidence: 99%

“…However, although S. cerevisiae may pose a potential problem in patients with compromised immune function (5), the antibody response in humans against this commonly considered innocuous yeast PPM remains ignored, as compared with what is known about responses to PPM from Candida albicans, an important opportunistic yeast pathogen (37). Studies of the C. albicans PPM oligomannosidic repertoire (7,13) reveal that oligomannosidic epitopes may be shared by a great number of different unrelated yeast molecules (34,41,42). The corresponding epitopes also occur over a wide variety of organisms, explaining immunological cross-reactivities among yeast species, yeast genera (10), filamentous fungi (14), viruses (27), bacteria (20,30), and human glycoproteins (22).…”

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confidence: 99%

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Specific antibody response to oligomannosidic epitopes in Crohn's disease

Sendid

Colombel

Jacquinot

et al. 1996

Clin Diagn Lab Immunol

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223

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Elevated antibody levels against the yeast Saccharomyces cerevisiae have been reported in sera from patients with Crohn's disease and not with ulcerative colitis. The aim of the study was to identify the nature of the epitopes supporting this antibody response. Whole cells from different S. cerevisiae strains were selected in immunofluorescence assay for their ability to differentiate the antibody responses of patients with Crohn's disease and ulcerative colitis. Their cell wall phosphopeptidomannans were then tested as antigen in enzymelinked immunosorbent assay (ELISA) against sera from 42 patients with Crohn's disease, 20 patients with ulcerative colitis, and 34 healthy controls. Graded chemical degradations were performed on the most reactive strain phosphopeptidomannan. The discriminating epitope was determined through gas-liquid chromatography-mass spectrometry. The greatest discrimination among patients with Crohn's disease, ulcerative colitis, and controls was obtained with Su1, a S. cerevisiae strain used in brewing of beer. ELISA directed against phosphopeptidomannan of this strain was 64% sensitive and 77% specific for discriminating Crohn's disease versus ulcerative colitis and 71% sensitive and 89% specific for Crohn's disease versus controls. Periodate oxidation and selective degradation demonstrated that the most important polysaccharide epitope was shared by both the acid-stable and the alkali-labile domains of the phosphopeptidomannan. The determination of oligomannose sequences of S. cerevisiae Su1 phosphopeptidomannans suggested that a mannotetraose, Man(133)Man(132)Man(132)Man, supported the serological response seen in Crohn's disease. Further identification of the immunogen eliciting this antibody response as a marker of the disease may help to understand its etiology.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Specific antibody response to oligomannosidic epitopes in Crohn's disease

Sendid

Colombel

Jacquinot

et al. 1996

Clin Diagn Lab Immunol

Self Cite

223

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“…They correspond to a large and complex repertoire of mannopyranose units linked by either ␣-1,6, ␣-1,3, ␣-1,2, or ␤-1,2 linkages (61). Among these units, oligomannose sequences corresponding to epitopes specific for human and animal antibodies, either polyclonal or monoclonal, have been identified; antibody recognition depends on both the type of linkage connecting the mannose units and the length of the mannose chain (17,19,22,32,47,61,65). These epitopes may also be shared by the glycosidic moiety of a large number of different mannoproteins or glycolipids, reinforcing the quantitatively major character of mannose residues in C. albicans cells (64,65).…”

mentioning

confidence: 99%

New Enzyme Immunoassays for Sensitive Detection of Circulating Candida albicans Mannan and Antimannan Antibodies: Useful Combined Test for Diagnosis of Systemic Candidiasis

et al. 1999

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Two standardized enzyme immunoassays for the serological diagnosis of candidiasis were developed. The first one detects antimannan antibodies, while the second one detects mannan with a sensitivity of 0.1 ng/ml. These tests were applied to 162 serum samples retrospectively selected from 43 patients with mycologically and clinically proven candidiasis caused by Candida albicans. Forty-three serum samples were positive for mannan, and 63 had significant antibody levels. Strikingly, only five serum samples were simultaneously positive by both tests. When the results were analyzed per patient, 36 (84%) presented at least one serum positive by one test. For 30 of them, positivity by one test was always associated with negative results by the other test for any of the tested sera. For six patients whose sera were positive for either an antigen or an antibody response, a balance between positivity by each test was evidenced by kinetic analysis of sera drawn during the time course of the infection. Controls consisted of 98 serum samples from healthy individuals, 93 serum samples from patients hospitalized in intensive care units, and 39 serum samples from patients with deep mycoses. The sensitivities and specificities were 40 and 98% and 53 and 94% for mannanemia or antibody detection, respectively. These values reached 80 and 93%, respectively, when the results of both tests were combined. These observations, which clearly demonstrate a disparity between circulation of a given mannan catabolite and antimannan antibody response, suggest that use of both enzyme immunoassays may be useful for the routine diagnosis of candidiasis.

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“…They have recently been shown to be involved in C. albicans binding to macrophages (25) and in the induction of cytokines (24). These residues support a specific antibody response in animals and humans (36,39,44,46). In C. albicans, ␤-1,2-oligomannosidic epitopes have been demonstrated to be expressed on a 14-to 18-kDa mannoglycoconjugate, corresponding to PLM, which electively presents this type of epitope (4,(45)(46)(47).…”

Section: Discussionmentioning

confidence: 99%

“…However, during the last decade, considerable fundamental data on mannan structure (16,42), antigenicity (16,31,38,42), and biological properties (11,17,33) have been accumulated. The synthesis of these data makes it clear that the sequences of mannose residues expressed in cell wall mannan are differently recognized by a mammal's immune system, depending on the anomer type of linkages between mannose residues, either ␣ or ␤ (25,31,36,44,46). Subsequently, with regard to antimannan antibodies, they can be roughly classified as anti-␣-and anti-␤-Man residues.…”

mentioning

confidence: 99%

Differential humoral response against alpha- and beta-linked mannose residues associated with tissue invasion by Candida albicans

Jouault

Delaunoy

Sendid

et al. 1997

Clin Diagn Lab Immunol

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Candida albicans mannan is the major cell wall antigen that elicits antibodies considered to be of little diagnostic value. It comprises epitopes corresponding to sequences of ␣-and ␤-1,2-linked mannose residues. Both types of oligomannosidic epitopes may also be present on the glycosidic portions of other C. albicans molecules, i.e., mannoproteins (MP) (either structural or enzymatic) and glycolipids. The human humoral responses against ␤-1,2-and ␣-linked oligomannosides were investigated by C. albicans Western blotting by considering the elective distribution of ␤-1,2-oligomannosidic epitopes over a 14-to 18-kDa phospholipomannan (PLM) and the presence of ␣-mannosidic epitopes over heavily glycosylated MP. Western blotting of 51 control sera confirmed the presence of antibodies against C. albicans as a commensal member of the indigenous microflora; an immunoglobulin G (IgG) reactivity linked to enzyme-linked immunosorbent assay mannan signals was found for both PLM (␤-1,2-Man residues) and MP (␣-Man residues). Despite strong reactivities against mannan and MP, IgG from 21 hospitalized patients with mycological evidence of deep-tissue invasion by C. albicans very significantly failed to react or reacted only faintly with PLM. This downregulation of anti-␤-1,2-oligomannosidic epitopes, associated with tissue invasion by C. albicans, was confirmed in 3 of 4 AIDS patients with extended oroesophageal candidosis. The application of a dissociation procedure proved that the absence of PLM reactivity was not due to the presence of immune complexes. These data provide the first evidence for a qualitative modification of the human antimannan antibody response associated with the C. albicans commensal-pathogenic transition.

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Probable presence of beta(1-2)-linked oligomannosides that act as human immunoglobulin G3 epitopes and are distributed over a Candida albicans 14- to 18-kilodalton antigen

Cited by 18 publications

References 9 publications

Specific antibody response to oligomannosidic epitopes in Crohn's disease

Specific antibody response to oligomannosidic epitopes in Crohn's disease

New Enzyme Immunoassays for Sensitive Detection of Circulating Candida albicans Mannan and Antimannan Antibodies: Useful Combined Test for Diagnosis of Systemic Candidiasis

Differential humoral response against alpha- and beta-linked mannose residues associated with tissue invasion by Candida albicans

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