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Expression and Purification of the Crystalline Surface Layer Protein of Rickettsia typhi
Author(s) -
Hahn MyongJoon,
Chang WooHyun
Publication year - 1996
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1996.tb03339.x
Subject(s) - rickettsia typhi , biology , microbiology and biotechnology , fusion protein , open reading frame , gene , polyclonal antibodies , murine typhus , maltose binding protein , antiserum , recombinant dna , escherichia coli , salmonella typhi , typhus , virology , peptide sequence , antigen , genetics
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.