AJTMH Tropical Medicine and Hygiene News
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am. J. Trop. Med. Hyg., 50(1), 1994, pp. 52-58
Copyright © 1994 by The American Society of Tropical Medicine and Hygiene

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chen, S.-M.
Right arrow Articles by Walker, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, S.-M.
Right arrow Articles by Walker, D. H.

Identification of the Antigenic Constituents of Ehrlichia chaffeensis

S.-M. Chen, J. S. Dumler, H.-M. Feng AND D. H. Walker
Department of Pathology, University of Texas Medical Branch, Galveston, Texas; Department of Pathology, University of Maryland School of Medicine, Baltimore, Maryland

Ehrlichia chaffeensis, the novel etiologic agent of human ehrlichiosis in the United States, was first isolated in 1990 and reported in 1991. To analyze the antigenic components of E. chaffeensis, we cultivated these obligate intracellular bacteria in DH82 cells, purified the ehrlichiae by renografin density gradient centrifugation, and examined the antigens by Western immunoblotting. Rabbit and human antisera to E. chaffeensis revealed more than 20 bands ranging from 20 to 200 kD. The distinct 22-kD protein was heat labile. The rest of the major immunoreactive components were heat stable. The immunoblots of E. chaffeensis were highly similar when probed with antisera to E. chaffeensis, E. canis, and E. ewingii, indicating the close antigenic relationships among the three species. The 22-kD protein cross-reacted only with anti-E. canis serum. The antibody against E. sennetsu reacted strongly with the 66-, 64-, 55-, and 44-kD antigens of E. chaffeensis. The E. risticii antisera reacted strongly with the 55- and 44-kD bands but only faintly with the 66-kD band. The major immunoreactive antigens of E. chaffeensis (66, 55, and 44 kD) showed cross-reactions with all the different antisera tested. The results indicated that E. chaffeensis is antigenically most closely related to E. canis, is less closely related to E. ewingii, and is only distantly related to E. sennetsu and E. risticii.




This article has been cited by other articles:


Home page
 Infect. Immun.Home page
T. Luo, X. Zhang, A. Wakeel, V. L. Popov, and J. W. McBride
A Variable-Length PCR Target Protein of Ehrlichia chaffeensis Contains Major Species-Specific Antibody Epitopes in Acidic Serine-Rich Tandem Repeats
Infect. Immun., April 1, 2008; 76(4): 1572 - 1580.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
Y. Ge and Y. Rikihisa
Surface-Exposed Proteins of Ehrlichia chaffeensis
Infect. Immun., August 1, 2007; 75(8): 3833 - 3841.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
S. M. Noh, K. A. Brayton, D. P. Knowles, J. T. Agnes, M. J. Dark, W. C. Brown, T. V. Baszler, and G. H. Palmer
Differential Expression and Sequence Conservation of the Anaplasma marginale msp2 Gene Superfamily Outer Membrane Proteins.
Infect. Immun., June 1, 2006; 74(6): 3471 - 3479.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1994 by the American Society of Tropical Medicine and Hygiene.