Characterization of epitopes recognized by Candida factor 1 and 9 antisera by use of Saccharomyces cerevisiae mnn mutants

Ataoglu, Haluk; Zueco, Jesús; Sentandreu, Rafael

doi:10.1128/iai.61.8.3313-3317.1993

Cited by 17 publications

(10 citation statements)

References 33 publications

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“…The slide agglutination assay with serum factors does not necessarily give quantitative results, as described by Ataoglu et al (1). Serum factor 1 has been shown to preferentially recognize the ␣-1,2-linked oligomannosyl side chains in mannan (1,10,23). The present results of the inhibition ELISAs against serum factor 1 also revealed the importance of ␣-linked oligomannosyl residues as antigenic serum factor 1.…”

Section: Discussionsupporting

confidence: 49%

“…The activity against serum factor 4 of the three acid-treated mannans, B-27-M-a, B-37-M-a, and B-37-27-M-a, may be due to the presence of branched side chains that dominate their antigenic serum factor 4 specificities (27). The slide agglutination assay with serum factors does not necessarily give quantitative results, as described by Ataoglu et al (1). Serum factor 1 has been shown to preferentially recognize the ␣-1,2-linked oligomannosyl side chains in mannan (1,10,23).…”

Section: Discussionmentioning

confidence: 99%

“…These three mannans retained 1-O-phosphorylated mannose units corresponding to 5.535 and 5.552 ppm. The amounts of the ␤-1,2mannopyranosyl unit and the phosphate groups increased in the order B-37-M, B-27-M, and B-37-27-M. 1 H NMR spectra also indicated a lack of ␤-1,2-linked oligomannosyl residues and 1-O-phosphorylated mannose units in the three acidtreated mannans (Fig. 3D).…”

Section: Characterization Of B-strain Culturesmentioning

confidence: 92%

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Antigenicity of cell wall mannans of Candida albicans NIH B-792 (serotype B) strain cells cultured at high temperature in yeast extract-containing sabouraud liquid medium

Okawa¹,

Goto²,

Nemoto³

et al. 1996

Clin Diagn Lab Immunol

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Cultivation of Candida albicans NIH B-792 (serotype B) at high temperature (37؇C) for 48 h in yeast extract-containing Sabouraud liquid medium (YSLM) provided the following findings in comparison with the findings obtained after incubation at 27؇C. Growth of the blastoconidia of this strain was decreased, with a dry weight of 9%, and the cells were deficient in cytokinesis. The cells did not undergo agglutination with serum factor 5 from a commercially available serum factor kit (Candida Check). Mannan (B-37-M) obtained from the cells cultured at 37؇C had partially lost its reactivity against serum factor 4 and lost most of its reactivity against serum factor 5 in an enzyme-linked immunosorbent assay (ELISA) in contrast to that (B-27-M) at 27؇C. Both cells and mannan prepared by cultivation first at 37؇C and then at 27؇C entirely recovered their reactivities with serum factors 4 and 5. 1 H-nuclear magnetic resonance analysis also revealed that B-37-M had lost a ␤-1,2-linked mannopyranose unit and retained a phosphate group. Similar changes were observed in the three other serotype B strains used in the study. The ␤-1,2-linked mannooligosaccharides longer than mannotetraose were not included among the products released from B-37-M by mild acid treatment. The results of the inhibition ELISA with a series of ␤-1,2-linked mannooligosaccharides from biose to octaose (M2 to M8, respectively) showed that the reactivity against serum factor 4 was inhibited most strongly by the oligosaccharides M4 to M8 and that the reactivity against serum factor 5 was inhibited completely by relatively longer oligosaccharides, M5 to M8, indicating their participation as the antigenic factor 5 epitopes.

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Section: Discussionsupporting

confidence: 49%

Section: Discussionmentioning

confidence: 99%

Section: Characterization Of B-strain Culturesmentioning

confidence: 92%

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Antigenicity of cell wall mannans of Candida albicans NIH B-792 (serotype B) strain cells cultured at high temperature in yeast extract-containing sabouraud liquid medium

Okawa¹,

Goto²,

Nemoto³

et al. 1996

Clin Diagn Lab Immunol

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“…The general features of cell wall mannoproteins in C. albicans are basically identical to those found for Saccharomyces cerevisiae, one of the most thoroughly investigated yeasts in this regard. Several studies have resulted in a detailed knowledge of the structure of this cell wall constituent in C. albicans (12,(262)(263)(264)(265)(494)(495)(496)(497)(498). Thus, mannose polymers are linked to the protein moiety through asparagine (by Nglycosidic bonds through two GlcNAc [di-N-acetylchitobiose] residues) and threonine or serine (by O-glycosidic, alkali-labile linkages) residues.…”

Section: Compositionmentioning

confidence: 99%

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Chaffin

López-Ribot

Casanova

et al. 1998

Microbiol Mol Biol Rev

655

344

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SUMMARY The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was intially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis.

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“…The major antigenic determinant in the outermost region of the C. albicans cell wall is mannoprotein (MP). This structure makes initial contact with the host (35) and participates in immunomodulation (1,3,8,20) and adherence (2, 10, 28-30, 37, 40, 52), and antimannan antibodies may be protective (17,18). Its major constituent is D-mannose, presented as N-linked (90%) and O-linked (10%) oligomannosides (5,19,39,54).…”

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confidence: 99%

Relative Abundance of Oligosaccharides in Candida Species as Determined by Fluorophore-Assisted Carbohydrate Electrophoresis

Goins

Cutler

2000

J Clin Microbiol

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Fluorophore-assisted carbohydrate electrophoresis (FACE) is a straightforward, sensitive method for determining the presence and relative abundance of individual oligomannosyl residues inCandida mannoprotein, the major antigenic determinant located on the outer surface of the yeast cell wall. The single terminal aldehydes of oligomannosyl residues released by hydrolysis were tagged with the charged fluorophore 8-aminonaphthalene-1,3,6-trisulfonate (ANTS) and separated with high resolution on the basis of size by polyacrylamide gel electrophoresis. ANTS fluorescence labeling was not biased by oligomannoside length; therefore, band fluorescence intensity was directly related to the relative abundance of individual oligomannoside moieties in heterogeneous samples. FACE analysis revealed the major oligomannosides released by acid hydrolysis and β-elimination of Fehling-precipitated mannan from Candida albicans, which were the same as those previously reported in studies based on mass and nuclear magnetic spectroscopic analysis. FACE was also amenable to the analysis of samples obtained by direct hydrolysis of whole yeast cells. Whole-cell acid hydrolysis and whole-cell β-elimination of two isolates each ofC. albicans, C. glabrata, C. krusei, C. lusitaniae, C. parapsilosis,C. rugosa, C. stellatoidea, and C. tropicalis resulted in oligomannoside gel banding patterns that were species and strain specific for the 16 isolates surveyed. Whereas some bands were specific for an individual isolate or species, other bands were shared by two or three species in various groupings. Differences in the mannoprotein composition of C. albicans A9 and four spontaneous cell surface mutants were also detected. Mannan “fingerprints,” or banding pattern profiles, derived from the electrophoretic mobilities of individual bands relative to the migration of acid-hydrolyzed dextran (relative migration index) yielded profiles characteristic of individual isolates not revealed by standard assimilation and biochemical profiles. FACE represents an accessible, sensitive, and quantitative analytical tool enabling the characterization of yeast mannan complexity.

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Characterization of epitopes recognized by Candida factor 1 and 9 antisera by use of Saccharomyces cerevisiae mnn mutants

Cited by 17 publications

References 33 publications

Antigenicity of cell wall mannans of Candida albicans NIH B-792 (serotype B) strain cells cultured at high temperature in yeast extract-containing sabouraud liquid medium

Antigenicity of cell wall mannans of Candida albicans NIH B-792 (serotype B) strain cells cultured at high temperature in yeast extract-containing sabouraud liquid medium

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Relative Abundance of Oligosaccharides in Candida Species as Determined by Fluorophore-Assisted Carbohydrate Electrophoresis

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