Characterization of a Species-specific Antigen in Rickettsia typhi.
- Author:
Soo Dong WOO
1
;
Chang Soon YOON
;
Jin Sang LEE
;
In Ae CHANG
;
Young Jin KIM
;
Song Woo SHIN
;
Hyun Jin JEON
;
Min Kee CHO
;
Yoon Won KIM
Author Information
1. Institute of Medical Science, College of Medicine, Hallym University, Chunchon, Korea. ywkim@hallym.ac.kr
- Publication Type:Original Article
- Keywords:
Murine typhus;
Rickettsia typhi;
Species-specific antigen
- MeSH:
Animals;
Antibodies, Monoclonal;
Blotting, Western;
Electrophoresis, Polyacrylamide Gel;
Epitopes;
Immune Sera;
Korea;
Mice;
Rickettsia typhi*;
Rickettsia*;
Typhus, Endemic Flea-Borne
- From:Journal of Bacteriology and Virology
2002;32(3):247-254
- CountryRepublic of Korea
- Language:Korean
-
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.
