Saccharomyces cerevisiae antibodies

Hunte, C., Koepke, J., Lange, C., Rossmanith, T. and Michel, H. (2000) Structure at 2.3 A resolution of the cytochrome bcj complex from the yeast Saccharomyces cerevisiae with an antibody Fv fragment, Structure, 8, 669-684. 

According to a review by Walsh [10], of 165 biopharmaceuhcal products approved in the United States and Europe by 2006, only two are nucleic acid-based drugs, whereas nine of the 31 therapeutic proteins approved since 2003 are produced in E, coli, and 17 are produced by mammalian cell lines. In 2004 market distribution and manufacture of therapeutic proteins, non-glycosylated (non-antibody) proteins constitutes 40% of the total market, with 12% armual growth rate, and are produced in E. coli or the yeast Saccharomyces cerevisiae glycoproteins (primarily mAbs) constitute 60% of the total market, with 26% armual growth rate, and are produced by mammalian cell culture (mostly with cells from Chinese Hamster Ovary, or CHO). 

Ito K, Ishiguro A, Kanbe T, Tanaka K, Torii S Detection of IgE antibody against Candida albicans enolase and its cross-reactivity to Saccharomyces cerevisiae enolase. Clin Exp Allergy 1995 25 522-528. 

J., Graff, C., Wiley, H. S. and Wittrup, K. D. (2003) Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Nat Biotechnol 21,163-170... 

Miller, K. D., Weaver-Feldhaus, J., Gray, S. A., Siegel, R. W., and Feldhaus, M. J. (2005) Production, purification, and characterization of human scFv antibodies expressed in Saccharomyces cerevisiae, Pichia pastoris, and Escherichia coli. Protein Expr Purif 42, 255-67... 

Yeast display uses the a-agglutinin receptor to display recombinant proteins on the surface of Saccharomyces cerevisiae. Yeast display of scFvs or Fabs allows the detection and selection by fluorescence-assisted flow cytometry or by magnetic sorting. In addition, flow cytometry can be used for kinetic characterization of antibody affinity (K ) as well as K ff and rates. ... 

The mannan subfractions of Saccharomyces cerevisiae, prepared by the similar chromatographic fractionation of the corresponding bulk mannan, showed no or very weak cross-reactivity with antisera of strains NIH A-207 and NIH B-792, while the mannan subfractions of strains NIH B-792 and J-1012 were weakly cross-reactive with anti-S. cerevisiae serum, affording almost identical amounts of precipitated antibody nitrogen regardless of the phosphate content of these mannan subfractions. 

This protocol was developed for yeast telomere hybridization experiments, in which we wished to localize both telomeric repeats and either RAPl protein or nuclear pore proteins. For such it has been most successful to fix the cells lightly, remove the cell wall, and carry out the immunofluorescence steps first. Following antibody staining, the cells can be postfixed and hybridized without loss of the immunofluorescence signal. The primary fixation method is based on the work done by Davis and colleagues (Davis and Fink, 1990 Loeb et al., 1993) to immunolocalize nuclear pore components in Saccharomyces cerevisiae. 

Zimarino V, Wilson S, Wu C (1990) Antibody-mediated activation of Drosophila heat shock factor in vitro. Science 249 546-549 Zitomer RS, Seller JW, McCarter DW, Hastings GA, Wick P, Lowry CV (1987) Elements involved in oxygen regulation of the Saccharomyces cerevisiae CYC7 gene. Mol Cell Biol 7 2212-2220... 

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