This Article
Right arrow Full Text
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by McBride, J. W.
Right arrow Articles by Walker, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McBride, J. W.
Right arrow Articles by Walker, D. H.

 Previous Article  |  Next Article 

Infection and Immunity, May 2003, p. 2516-2524, Vol. 71, No. 5
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.5.2516-2524.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Kinetics of Antibody Response to Ehrlichia canis Immunoreactive Proteins

Jere W. McBride,1,2,3* Richard E. Corstvet,4,5 Steven D. Gaunt,4 Charles Boudreaux,5 Thaya Guedry,4 and David H. Walker1,2,3

Department of Pathology,1 Sealy Center for Vaccine Developmentthe,2 Center for Biodefense and Emerging Infectious Diseases, University of Texas Medical Branch, Galveston, Texas 77555-0609,3 Department of Veterinary Pathobiological Sciences, School of Veterinary Medicine,4 Department of Veterinary Science, Louisiana State University, Baton Rouge, Louisiana 70803-00015

Received 12 December 2002/ Returned for modification 6 February 2003/ Accepted 14 February 2003

Immunoreactive proteins of Ehrlichia canis and Ehrlichia chaffeensis that have been characterized include a family of 28-kDa major outer membrane proteins (p28) and two large antigenically divergent surface glycoprotein orthologs. We previously demonstrated that recombinant E. canis p28 and the 140- and 200-kDa glycoproteins gp140 and gp200, respectively, react strongly with serum antibodies from suspect canine ehrlichiosis cases that were positive for E. canis by immunofluorescent antibody test and in various phases of acute or chronic infection (J. Clin. Microbiol. 39:315-322, 2001). The kinetics of the antibody response to these potentially important vaccine and immunodiagnostic candidates is not known. Acute-phase serum antibody responses to whole-cell E. canis lysates and recombinant p28, gp140, and gp200 were monitored for 6 weeks in dogs experimentally infected with E. canis. Irrespective of the inoculation route, a T-helper 1-type response was elicited to E. canis antigens consisting of immunoglobulin G2 antibodies exclusively in both acute and convalescent phases in most dogs. Analysis of immuoreactive antigens for peak intensity and relative quantity identified major immunoreactive E. canis antigens recognized early in the infection as the 19-, 37-, 75-, and 140-kDa proteins. Later in infection, additional major immunoreactive E. canis proteins were identified, including the 28-, 47-, and 95-kDa proteins and the recently identified 200-kDa glycoprotein. All dogs had developed antibody against the recombinant gp140, gp200, and p28 in the convalescent phase. Immunoreactivity and antibody response kinetics suggest that major immunoreactive proteins identified are immunodominant, but early recognition suggests increased dominance by some antigens.

* Corresponding author. Mailing address: Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555-0609. Phone: (409) 772-4813. Fax: (409) 747-2415. E-mail: jemcbrid{at}utmb.edu.

Editor: W. A. Petri, Jr.

Infection and Immunity, May 2003, p. 2516-2524, Vol. 71, No. 5
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.5.2516-2524.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zhu, B., Nethery, K. A., Kuriakose, J. A., Wakeel, A., Zhang, X., McBride, J. W. (2009). Nuclear Translocated Ehrlichia chaffeensis Ankyrin Protein Interacts with a Specific Adenine-Rich Motif of Host Promoter and Intronic Alu Elements. Infect. Immun. 77: 4243-4255 [Abstract] [Full Text]  
  • Luo, T., Zhang, X., McBride, J. W. (2009). Major Species-Specific Antibody Epitopes of the Ehrlichia chaffeensis p120 and E. canis p140 Orthologs in Surface-Exposed Tandem Repeat Regions. CVI 16: 982-990 [Abstract] [Full Text]  
  • Wakeel, A., Kuriakose, J. A., McBride, J. W. (2009). An Ehrlichia chaffeensis Tandem Repeat Protein Interacts with Multiple Host Targets Involved in Cell Signaling, Transcriptional Regulation, and Vesicle Trafficking. Infect. Immun. 77: 1734-1745 [Abstract] [Full Text]  
  • Zhang, X., Luo, T., Keysary, A., Baneth, G., Miyashiro, S., Strenger, C., Waner, T., McBride, J. W. (2008). Genetic and Antigenic Diversities of Major Immunoreactive Proteins in Globally Distributed Ehrlichia canis Strains. CVI 15: 1080-1088 [Abstract] [Full Text]  
  • Luo, T., Zhang, X., Wakeel, A., Popov, V. L., McBride, J. W. (2008). A Variable-Length PCR Target Protein of Ehrlichia chaffeensis Contains Major Species-Specific Antibody Epitopes in Acidic Serine-Rich Tandem Repeats. Infect. Immun. 76: 1572-1580 [Abstract] [Full Text]  
  • Nethery, K. A., Doyle, C. K., Zhang, X., McBride, J. W. (2007). Ehrlichia canis gp200 Contains Dominant Species-Specific Antibody Epitopes in Terminal Acidic Domains. Infect. Immun. 75: 4900-4908 [Abstract] [Full Text]  
  • Ge, Y., Rikihisa, Y. (2007). Surface-Exposed Proteins of Ehrlichia chaffeensis. Infect. Immun. 75: 3833-3841 [Abstract] [Full Text]  
  • Cardenas, A. M., Doyle, C. K., Zhang, X., Nethery, K., Corstvet, R. E., Walker, D. H., McBride, J. W. (2007). Enzyme-Linked Immunosorbent Assay with Conserved Immunoreactive Glycoproteins gp36 and gp19 Has Enhanced Sensitivity and Provides Species-Specific Immunodiagnosis of Ehrlichia canis Infection. CVI 14: 123-128 [Abstract] [Full Text]  
  • McBride, J. W., Doyle, C. K., Zhang, X., Cardenas, A. M., Popov, V. L., Nethery, K. A., Woods, M. E. (2007). Identification of a Glycosylated Ehrlichia canis 19-Kilodalton Major Immunoreactive Protein with a Species-Specific Serine-Rich Glycopeptide Epitope. Infect. Immun. 75: 74-82 [Abstract] [Full Text]  
  • Mavromatis, K., Doyle, C. K., Lykidis, A., Ivanova, N., Francino, M. P., Chain, P., Shin, M., Malfatti, S., Larimer, F., Copeland, A., Detter, J. C., Land, M., Richardson, P. M., Yu, X. J., Walker, D. H., McBride, J. W., Kyrpides, N. C. (2006). The Genome of the Obligately Intracellular Bacterium Ehrlichia canis Reveals Themes of Complex Membrane Structure and Immune Evasion Strategies. J. Bacteriol. 188: 4015-4023 [Abstract] [Full Text]  
  • Doyle, C. K., Nethery, K. A., Popov, V. L., McBride, J. W. (2006). Differentially Expressed and Secreted Major Immunoreactive Protein Orthologs of Ehrlichia canis and E. chaffeensis Elicit Early Antibody Responses to Epitopes on Glycosylated Tandem Repeats. Infect. Immun. 74: 711-720 [Abstract] [Full Text]  
  • Doyle, C. K., Zhang, X., Popov, V. L., McBride, J. W. (2005). An Immunoreactive 38-Kilodalton Protein of Ehrlichia canis Shares Structural Homology and Iron-Binding Capacity with the Ferric Ion-Binding Protein Family. Infect. Immun. 73: 62-69 [Abstract] [Full Text]  
  • Olano, J. P., Wen, G., Feng, H.-M., McBride, J. W., Walker, D. H. (2004). Histologic, Serologic, and Molecular Analysis of Persistent Ehrlichiosis in a Murine Model. Am. J. Pathol. 165: 997-1006 [Abstract] [Full Text]  
  • Ismail, N., Soong, L., McBride, J. W., Valbuena, G., Olano, J. P., Feng, H.-M., Walker, D. H. (2004). Overproduction of TNF-{alpha} by CD8+ Type 1 Cells and Down-Regulation of IFN-{gamma} Production by CD4+ Th1 Cells Contribute to Toxic Shock-Like Syndrome in an Animal Model of Fatal Monocytotropic Ehrlichiosis. J. Immunol. 172: 1786-1800 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»