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Wadle, A; Mischo, A; Strahl, S; Nishikawa, H; Held, G; Neumann, F; Wullner, B; Fischer, E; Kleber, S; Karbach, J; Jager, E; Shiku, H; Odunsi, K; Shrikant, P A; Knuth, A; Cerundolo, V; Renner, C (2010). NY-ESO-1 protein glycosylated by yeast induces enhanced immune responses. FEMS Yeast Research, 27(11):919-931.

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Vaccine strategies that target dendritic cells to elicit potent cellular immunity are the subject of intense research. Here we report that the genetically engineered yeast Saccharomyces cerevisiae, expressing the full-length tumour-associated antigen NY-ESO-1, is a versatile host for protein production. Exposing dendritic cells (DCs) to soluble NY-ESO-1 protein linked to the yeast a-agglutinin 2 protein (Aga2p) protein resulted in protein uptake, processing and MHC class I cross-presentation of NY-ESO-1-derived peptides. The process of antigen uptake and cross-presentation was dependent on the glycosylation pattern of NY-ESO-1-Aga2p protein and the presence of accessible mannose receptors. In addition, NY-ESO-1-Aga2p protein uptake by dendritic cells resulted in recognition by HLA-DP4 NY-ESO-1-specific CD4(+) T cells, indicating MHC class II presentation. Finally, vaccination of mice with yeast-derived NY-ESO-1-Aga2p protein led to an enhanced humoral and cellular immune response, when compared to the bacterially expressed NY-ESO-1 protein. Together, these data demonstrate that yeast-derived full-length NY-ESO-1-Aga2p protein is processed and presented efficiently by MHC class I and II complexes and warrants clinical trials to determine the potential value of S. cerevisiae as a host for cancer vaccine development.


2 citations in Web of Science®
3 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Clinic for Oncology
Dewey Decimal Classification:610 Medicine & health
Deposited On:18 Jan 2011 11:28
Last Modified:05 Apr 2016 14:25
Additional Information:The definitive version is available at www.blackwell-synergy.com
Publisher DOI:10.1002/yea.1796
PubMed ID:20672253

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