Journal article

Publication year: 1995

Pages: 205-212

Journal: Journal of Biotechnology

Volume number: 43

Issue number: 3

ISSN: 0168-1656

DOI Link: https://doi.org/10.1016/0168-1656(95)00138-7

Publisher: Elsevier

Abstract: 
Listeriolysin, the hemolysin of the pathogenic species Listeria monocytogenes, was expressed in the non-pathogenic species Listeria innocua. Coexpression of the positive regulatory factor prfA in the plasmid vector in conjunction with the structural gene hly increased the expression over 500-fold. Purification from supernatant fluids was achieved by two steps of ion exchange chromatography. The procedure resulted in over 60% yield of a hemolytically active, homogenous 58 kDa protein which was used to produce monospecific antibodies. As shown by immunoblot the purified listeriolysin was free of p60, a highly immunogenic protein of similar size also produced by Listeria spp., which otherwise would interfere with immunoassays. Listeriolysin retained full activity for more than 6 months at - 70 degrees C.

Harvard Citation style: Darji, A., Chakraborty, T., Niebuhr, K., Tsonis, N., Wehland, J. and Weiss, S. (1995) Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification, Journal of Biotechnology, 43(3), pp. 205-212. https://doi.org/10.1016/0168-1656(95)00138-7

APA Citation style: Darji, A., Chakraborty, T., Niebuhr, K., Tsonis, N., Wehland, J., & Weiss, S. (1995). Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification. Journal of Biotechnology. 43(3), 205-212. https://doi.org/10.1016/0168-1656(95)00138-7