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Applied and Environmental Microbiology, February 2008, p. 1039-1049, Vol. 74, No. 4
0099-2240/08/$08.00+0 doi:10.1128/AEM.01547-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
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Department of Food Science and Biotechnology, National Chung-Hsing University, Taichung, Taiwan, Republic of China
Received 9 July 2007/ Accepted 11 December 2007
Bacillus subtilis and Lactococcus lactis are ideal hosts for the production of extracellular heterologous proteins of major commercial importance. A recombinant gene for the novel Ganoderma lucidium immunomodulatory protein LZ-8, recombinant LZ-8, was designed encoding the same amino acid sequence but using the preferred codons for both strains and was synthesized by overlapping extension PCR. Using the signal peptide (SP) from subtilisin YaB (SPYaB), recombinant LZ-8 was expressed extracellularly in Bacillus subtilis and Lactococcus lactis. In the absence of SPYaB, recombinant LZ-8 was expressed extracellularly in B. subtilis, but not in L. lactis. The three expressed recombinant LZ-8s showed different capacities for modulating the production of Th1 and Th2 cytokines by peripheral blood mononuclear cells and of tumor necrosis factor alpha by a macrophage cell line.
Published ahead of print on 21 December 2007.
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