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Signal peptide of Arabinosidase enhances secretion of interferon-α2b protein by Bifidobacteria longum

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Abstract

Bifidobacteria can potentially be used for gene therapy. Here, we reported that 65% of the total hIFN-α2b produced from Bifidobacteria longum transformed with pBAD-SPIFN plasmids encoding a fusion protein of the arabinosidase signal peptide and human IFN-α2b (hIFN-α2b), was secreted. For B. longum transformed with pBAD-IFN plasmids (hIFN-α2b without the signal peptide), only 15% of the total IFN-α2b was secreted and western blotting and N-terminal amino-acid sequence analysis revealed cleavage of the arabinosidase signal peptide from the secreted hIFN-α2b. Moreover, the active level of the secreted hIFN-α2b in the supernatant of B. longum transformed with pBAD-SPIFN plasmids was over 1,000 IU/ml commercial rhIFN-α2b. Hence, the arabinosidase signal peptide can enhance the secretion efficiency of IFN-α2b from B. longum.

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Acknowledgments

We thank Yulin Liu, Department of Cellular Biology of Southern Medical University, for kind help of N-terminal amino-acids sequence analysis of hIFN-α2b. This work was supported by a grant from Shenzhen scientific Research Program of the People’s Republic of China (NO. 200801020).

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Correspondence to Qiwen Deng or Weiseng Zeng.

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Communicated by Jorge Membrillo-Hernández.

Q. Deng, W. Zeng and Z. Yu contributed equally to this work.

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Deng, Q., Zeng, W. & Yu, Z. Signal peptide of Arabinosidase enhances secretion of interferon-α2b protein by Bifidobacteria longum . Arch Microbiol 191, 681–686 (2009). https://doi.org/10.1007/s00203-009-0496-5

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  • DOI: https://doi.org/10.1007/s00203-009-0496-5

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