ArticleInfection and immunity1997
Biochemical characterization of Candida albicans epitopes that can elicit protective and nonprotective antibodies.
Article in Infection and immunity, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
53 citing papers in PubMed, 149 citations in OpenAlex.
- Antifungal Innate Immunity.Advances in experimental medicine and biology · 2025Review
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- Antibodies as Models and Tools to DecipherJournal of fungi (Basel, Switzerland) · 2023Review
- Immunoglobulins at the interface of the gut mycobiota and anti-fungal immunity.Seminars in immunology · 2023Review
- The Role of B-Cells and Antibodies againstVaccines · 2021Review
- Customized yeast cell factories for biopharmaceuticals: from cell engineering to process scale up.Microbial cell factories · 2021Review
- Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes.Scientific reports · 2021Article
- Engineering of Yeast Glycoprotein Expression.Advances in biochemical engineering/biotechnology · 2021Article
- Monoclonal Antibodies as Tools to Combat Fungal Infections.Journal of fungi (Basel, Switzerland) · 2020Review
- Design of a mimotope-peptide based double epitope vaccine against disseminated candidiasis.Vaccine · 2019Article
- Article
- Engineering yeast for producing human glycoproteins: where are we now?Future microbiology · 2015Article
- Emerging drugs and vaccines for candidemia.Mycoses · 2014Review
- Discovery of two β-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514.PloS one · 2014Article
- Immunoglobulins in defense, pathogenesis, and therapy of fungal diseases.Cell host & microbe · 2012Review
- Article
- Vaccine and monoclonal antibody that enhance mouse resistance to candidiasis.Clinical and vaccine immunology : CVI · 2011Article
- Glycosylation status of the C. albicans cell wall affects the efficiency of neutrophil phagocytosis and killing but not cytokine signaling.Medical mycology · 2011Article
- Horizontal transmission of Candida albicans and evidence of a vaccine response in mice colonized with the fungus.PloS one · 2011Article
- Influence of mannan and glucan on complement activation and C3 binding by Candida albicans.Infection and immunity · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We previously reported that the immunoglobulin M (IgM) monoclonal antibody (MAb) B6.1 protects mice against disseminated candidiasis, whereas the IgM MAb B6 does not. Both MAbs are specific for an adhesin fraction isolated from the cell surface of Candida albicans, but their epitope specificities differ. In the present study, we examined the surface locations of both epitopes and obtained structural information regarding the B6.1 epitope. Immunofluorescence confocal microscopic analysis of C. albicans yeast forms showed that epitope B6.1 is displayed rather homogeneously over the entire cell surface, whereas epitope B6 appears to have a patchy distribution. Both antibodies were essentially nonreactive with the surfaces of mycelial forms of the fungus, indicating that neither epitope is expressed on the surfaces of these forms. For isolation of the B6.1 epitope, the adhesin fraction consisting of cell surface phosphomannan was subjected to mildly acidic (10 mM HCl) hydrolysis and was fractionated into acid-labile and acid-stable portions by size exclusion chromatography. Antibody blocking experiments showed that the B6.1 epitope is an acid-labile moiety of the phosphomannan and that the B6 epitope is located in the acid-stable fraction. The B6 epitope appeared to be mannan because it was stable to heat (boiling) and protease treatments but was destroyed by alpha-mannosidase digestion. The B6.1 epitope eluted from the size exclusion column in two fractions. Mass spectroscopic analyses showed that one fraction contained material with the size of a mannotriose and that the other was a mixture of mannotriose- and mannotetraose-size substances. Dose response inhibition tests of the fractions indicated that the B6.1 epitope is associated with the mannotriose. Nuclear magnetic resonance (NMR) spectroscopic analysis of the epitope yielded data consistent with a beta-(1-->2)-linked mannotriose. The fine structure of the B6 epitope is under investigation. Information derived from these investigations will be useful both in understanding protective versus nonprotective antibody responses to C. albicans and in improving anti-Candida vaccine formulations.
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