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J Bacteriol Virol. 2002 Sep;32(3):247-254. Korean. Original Article.
Woo SD , Yoon CS , Lee JS , Chang IA , Kim YJ , Shin SW , Jeon HJ , Cho MK , Kim YW , .
Institute of Medical Science, College of Medicine, Hallym University, Chunchon, Korea. ywkim@hallym.ac.kr
Department of Microbiology, College of Medicine, Hallym University, Chunchon, Korea.
ImmuneMed Inc., Chunchon, Korea.
Abstract

Murine typhus is an acute febrile illness caused by Rickettsia typhi. It is one of the four major acute febrile illnesses in Korea during autumn. To study a species-specific antigen of R. typhi, two clinical isolates (87-91 and 87-100) and two reference strains (VR-144 and VR-738) were analyzed by mouse antisera and monoclonal antibodies (MAbs). On SDS- polyacrylamide gel electrophoresis (PAGE), R. typhi showed major antigen bands of 135, 80, 75, 64, 47, 22, and 19 kDa and these bands differed with those of other species. On Western blot analysis, the MAbs reacting only with R. typhi could only detect 135 kDa protein. The 135 kDa protein appeared to be the species-specific antigen. Other MAbs showing cross-reactivity with R. prowazekii reacted with 135 kDa protein in fresh culture supernatant of R. typhi infected host cell. However, the cross-reacting antibody did also react with smaller protein bands, most of which seem to be degradation products of the 135 kDa protein since they increase in old protein stocks purified from R. typhi harvested from infected host cell. These suggest that 135 kDa protein is unstable and the R. typhi specific epitopes are located at the regions of 135 kDa protein that are removed when the protein is degraded. The 135 kDa protein or its specific and stable recombinant protein would serve an important target for the development of vaccine and specific diagnostic antigen.

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