Open AccessExpression and secretion of outer surface protein (OSP‐A) of Borrelia burgdorferi from Escherichia coli
Author(s) -
Chang YungFu,
Lauderdale TsaiLing,
Lee Woo Y.,
Shin Sang J.,
Jacobson Richard H.,
Appel Max J.,
Lein Donald H.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06184.x
Subject(s) - escherichia coli , borrelia burgdorferi , secretion , fusion protein , biology , microbiology and biotechnology , enterobacteriaceae , cloning (programming) , fusion gene , gene , biochemistry , recombinant dna , antibody , genetics , computer science , programming language
Outer surface protein A (OspA) is encoded by the ospA gene from Borrelia burgdorferi . This protein induces immunity against infection in mice. The cloning and expression of OspA in Escherichia coli have been previously described, but the secretion of OspA into culture media in E. coli has not yet been reported. In this report we demonstrate that a chimeric OspA protein was secreted into culture media by E. coli when it also harbors the hemolysin secretion genes hlyBD . The OspA fusion protein was also overexpressed from a T7 promoter and purified by immobilized metal ion chromatography. This was possible because the fusion protein contains ix histidyl residues in its N‐terminus.