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Expression and purification of the crystalline surface layer protein of Rickettsia typhi.

作者信息

Hahn M J, Chang W H

机构信息

Department of Microbiology, Kon-Kuk University, Choongju, South Korea.

出版信息

Microbiol Immunol. 1996;40(3):233-6. doi: 10.1111/j.1348-0421.1996.tb03339.x.

DOI:10.1111/j.1348-0421.1996.tb03339.x
PMID:8934678
Abstract

The crystalline surface layer (S-layer) protein (SLP) of Rickettsia typhi is known as the protective antigen against murine typhus. We previously reported a cloning and sequence analysis of the SLP gene of R. typhi (slpT) and showed that the open reading frame of this gene encodes both the SLP and a 32-kDa protein. To express only the SLP from this gene, the putative signal sequence and the 32-kDa protein portion were removed from the slpT. This protein was expressed in Escherichia coli as a fusion protein, consisting of the SLP and maltose binding protein. The recombinant protein reacted strongly with polyclonal antiserum of a patient with murine typhus.

摘要

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