ArticleInfection and immunity1996
Purification and biochemical characterization of a 65-kilodalton mannoprotein (MP65), a main target of anti-Candida cell-mediated immune responses in humans.
Article in Infection and immunity, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 81 citations in OpenAlex.
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- Insight Into the Properties and Immunoregulatory Effect of Extracellular Vesicles Produced byFrontiers in cellular and infection microbiology · 2022Article
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- Mass Spectrometry-Based Proteomic and Immunoproteomic Analyses of theJournal of fungi (Basel, Switzerland) · 2021Article
- The Role ofFrontiers in cellular and infection microbiology · 2021Review
- Protective effect of fungal extracellular vesicles against murine candidiasis.Cellular microbiology · 2020Article
- Antibodies against a β-glucan-protein complex of Candida albicans and its potential as indicator of protective immunity in candidemic patients.Scientific reports · 2017Article
- A computational model for regulation of nanoscale glucan exposure in Candida albicans.PloS one · 2017Article
- A Murine, Bispecific Monoclonal Antibody Simultaneously Recognizing β-Glucan and MP65 Determinants in Candida Species.PloS one · 2016Article
- Extracellular Vesicle-Associated Transitory Cell Wall Components and Their Impact on the Interaction of Fungi with Host Cells.Frontiers in microbiology · 2016Review
- The MP65 gene is required for cell wall integrity, adherence to epithelial cells and biofilm formation in Candida albicans.BMC microbiology · 2011Article
- New approach for diagnosis of candidemia based on detection of a 65-kilodalton antigen.Clinical and vaccine immunology : CVI · 2009Article
- The role of the cell wall in fungal pathogenesis.Microbial biotechnology · 2009Review
- Effect of tunicamycin on Candida albicans biofilm formation and maintenance.The Journal of antimicrobial chemotherapy · 2009Article
- Article
- Beta-1,2 oligomannose adhesin epitopes are widely distributed over the different families of Candida albicans cell wall mannoproteins and are associated through both N- and O-glycosylation processes.Infection and immunity · 2008Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 65 kDa-constituent (MP65) of a whole-cell mannoprotein (MP) fraction of Candida albicans was purified by immunoaffinity chromatography with monoclonal antibodies directed against periodate-insensitive, protease-sensitive MP epitopes, putatively polypeptide in nature. These antibodies were obtained by immunization of mice with concanavalin A bead-coupled, low-glycosylated MP from hyphal cells of C. albicans grown in the presence of a subinhibitory dose of tunicamycin. The immunoaffinity-purified MP65 molecule had a pI of 4.1 and a protein/polysaccharide ratio of 1.8:1. It was resistant to hydrolysis by endoglycosidase H, endoglycosidase F, or N-glycoffanases but still reactive with concanavalin A. The polysaccharide moiety of MP65 was composed exclusively of mannose and glucose at a ratio of 12.7 to 1. The protein moiety showed numerous potential O-glycosidic linkage sites as suggested by the high proportion of serine and threonine (together accounting for more than 20% of the total amino acid composition) and susceptibility to diluted alkali. This treatment and digestion with alpha-mannosidase caused a reduction in the MP65 molecular mass to around 54 kDa. The N-terminal sequence of MP65 protein moiety was rich in alanine and valine (7 of 13 amino acids) and did not show any significant homology with deposited sequences in data banks. Purified MP65, at doses of a few nanograms, induced extensive T-cell proliferation of human peripheral blood mononuclear cells. This proliferation was specifically inhibited, in a dose-response fashion, by the antigen-binding fragment of the monoclonal antibody used for immunoaffinity purification. Overall, these results highlight biochemical and molecular details of MP65, a main target of human T-cell response to C.albicans.
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