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Clinical and Vaccine Immunology, July 2009, p. 982-990, Vol. 16, No. 7
1071-412X/09/$08.00+0     doi:10.1128/CVI.00048-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Major Species-Specific Antibody Epitopes of the Ehrlichia chaffeensis p120 and E. canis p140 Orthologs in Surface-Exposed Tandem Repeat Regions{triangledown}

Tian Luo,1 Xiaofeng Zhang,1 and Jere W. McBride1,2,3,4,5*

Departments of Pathology,1 Microbiology and Immunology,2 Center for Biodefense and Emerging Infectious Diseases,3 Sealy Center for Vaccine Development,4 Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, Texas 775555

Received 3 February 2009/ Returned for modification 24 February 2009/ Accepted 24 April 2009

Ehrlichia chaffeensis and E. canis have a small subset of tandem repeat (TR)-containing protein orthologs, including p120/p140, which elicit strong antibody responses. The TR regions of these protein orthologs are immunoreactive, but the molecular characteristics of the p120/p140 epitopes have not been determined. In this study, the immunodeterminants of the E. chaffeensis p120 and E. canis p140 were identified and molecularly defined. Major antibody epitope-containing regions of both p120 and p140 were localized to the TR regions, which reacted strongly by Western immunoblotting with antibodies in sera from E. chaffeensis-infected dogs or patients and E. canis-infected dogs, respectively. Single continuous species-specific major epitopes within the E. chaffeensis p120 and E. canis p140 TRs were mapped to homologous surface-exposed glutamate/aspartate-rich regions (19 to 22 amino acids). In addition, minor cross-reactive epitopes were localized to homologous N- and C-terminal regions of p120 and p140. Furthermore, although the native and recombinant p120 and p140 proteins exhibited higher-than-predicted molecular masses, posttranslational modifications were not present on abnormally migrating p120 and p140 TR recombinant proteins as determined by matrix-assisted laser desorption ionization-time of flight mass spectrometry.

* Corresponding author. Mailing address: Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555-0609. Phone: (409) 747-2498. Fax: (409) 747-2455. E-mail: jemcbrid{at}utmb.edu

{triangledown} Published ahead of print on 6 May 2009.

Clinical and Vaccine Immunology, July 2009, p. 982-990, Vol. 16, No. 7
1071-412X/09/$08.00+0     doi:10.1128/CVI.00048-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Luo, T., Zhang, X., Nicholson, W. L., Zhu, B., McBride, J. W. (2010). Molecular Characterization of Antibody Epitopes of Ehrlichia chaffeensis Ankyrin Protein 200 and Tandem Repeat Protein 47 and Evaluation of Synthetic Immunodeterminants for Serodiagnosis of Human Monocytotropic Ehrlichiosis. CVI 17: 87-97 [Abstract] [Full Text]  


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