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High-level expression of Aspergillus niger b-galactosidase in Ashbya gossypii.

Ashbya gossypii has been recently considered as a host for the expression of recombinant proteins. The production levels achieved thus far were similar to those obtained with Saccharomyces cerevisiae for the same proteins. Here, the b-galactosidase from Aspergillus niger was successfully expressed and secreted by A. gossypii from 2-mm plasmids carrying the native signal sequence at higher levels than those secreted by S. cerevisiae laboratorial strains. Four different constitutive promoters were used to regulate the expression of bgalactosidase: A. gossypii AgTEF and AgGPD promoters, and S. cerevisiae ScADH1 and ScPGK1 promoters. The native AgTEF promoter drove the highest expression levels of recombinant b-galactosidase in A. gossypii, leading to 2- and 8-fold higher extracellular activity than the AgGPD promoter and the heterologous promoters, respectively. In similar production conditions, the levels of active b-galactosidase secreted by A. gossypii were up to 37 times higher than those secreted by recombinant S. cerevisiae and 2.5 times higher than those previously reported for the b-galactosidase-high producing S. cerevisiae NCYC869-A3/pVK1.1. The substitution of glucose by glycerol in the production medium led to a 1.5-fold increase in the secretion of active b-galactosidase by A. gossypii. Recombinant b-galactosidase secreted by A. gossypii was extensively glycosylated, as are the native A. niger b-galactosidase and recombinant b-galactosidase produced by yeast. These results highlight the potential of A. gossypii as a recombinant protein producer and open new perspectives to further optimize recombinant protein secretion in this fungus.

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Delivery of adenoviral DNA to mouse liver.

The liver represents a major target organ for gene delivery owing to its high biosynthetic capacity and access to the bloodstream. Adenoviral vectors are highly efficient gene-transfer vehicles, making them among the most promising systems for in vivo gene transfer to the liver. Following intravenous administration of adenoviral vectors to a variety of mammalian models, including mice, dogs, and monkeys, hepatocytes are efficiently transduced. Several delivery methods to the liver have been described, including portal vein (2-4), hepatic artery (3,5), and peripheral vein infusions (6). This chapter describes the simple, nonsurgical method of intravenous (iv) administration of adenoviral vectors in mice, and an immunohistochemical method to qualitatively evaluate liver transduction efficiency following delivery of an adenoviral vector encoding a bgalactosidase (beta-gal) marker gene. Additionally, several alternative methods to verify efficient liver transduction are introduced.

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Oestrogenic activity of CPRG (chlorophenol red-β-D-galactopyranoside), a β-galactosidase substrate commonly used in recombinant yeast oestrogenic assays.

The finding that a variety of chemicals display oestrogenic activity has resulted in the development of in vitro and in vivo assays to assess oestrogenic activity. One such assay, the yeast oestrogen assay (YES) makes use of recombinant yeast cells that harbour an oestrogen receptor expression cassette and a reporter construct, coding for bgalactosidase. The induction mechanism starts with the binding of oestrogenic compounds to the oestrogen receptor. This complex activates the production of β-galactosidase. The β-galactosidase activity is thus a measure of the oestrogenic activity of chemical compounds. In the YES assay, the β-galactosidase activity may be quantified with the chromogenic substrate chlorophenol red-β-d-galactopyranoside (CPRG). In the present study it is reported that CPRG or its β-galactosidase degradation product chlorophenol red act in the YES as an oestrogenic compound itself. The implications of this finding are described. It is especially argued that chlorophenol red production after prolonged incubation of the assay might be misinterpreted as an oestrogenic effect of the test compound.

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