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Infection and Immunity, August 2007, p. 3833-3841, Vol. 75, No. 8
0019-9567/07/$08.00+0     doi:10.1128/IAI.00188-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Surface-Exposed Proteins of Ehrlichia chaffeensis{triangledown} ,{dagger}

Yan Ge and Yasuko Rikihisa*

Department of Veterinary Biosciences, The Ohio State University, Columbus, OH 43210

Received 5 February 2007/ Returned for modification 12 March 2007/ Accepted 14 May 2007

The surface proteins of Ehrlichia chaffeensis provide an important interface for pathogen-host interactions. To investigate the surface proteins of E. chaffeensis, membrane-impermeable, cleavable Sulfo-NHS-SS-Biotin was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin-agarose affinity purification. The affinity-captured proteins were separated by electrophoresis, and five relatively abundant protein bands containing immunoreactive proteins were subjected to capillary-liquid chromatography-nanospray tandem mass spectrometry analysis. Nineteen out of 22 OMP-1/P28 family proteins, including P28 (which previously was shown to be surface exposed), were detected in E. chaffeensis cultured in human monocytic leukemia THP-1 cells. For the first time, with the exception of P28 and P28-1, 17 OMP-1/P28 family proteins were demonstrated to be expressed at the protein level. The surface exposure of OMP-1A and OMP-1N was verified by immunofluorescence microscopy. OMP-1B was undetectable either by surface biotinylation or by Western blotting of the whole bacterial lysate, suggesting that it is not expressed by E. chaffeensis cultured in THP-1 cells. Additional E. chaffeensis surface proteins detected were OMP85, hypothetical protein ECH_0525 (here named Esp73), immunodominant surface protein gp47, and 11 other proteins. The identification of E. chaffeensis surface-exposed proteins provides novel insights into the E. chaffeensis surface and lays the foundation for rational studies on pathogen-host interactions and vaccine development.

* Corresponding author. Mailing address: Department of Veterinary Biosciences, College of Veterinary Medicine, The Ohio State University, 1925 Coffey Rd., Columbus, OH 43210. Phone: (614) 292-5661. Fax: (614) 292-6473. E-mail: rikihisa.1{at}osu.edu

{triangledown} Published ahead of print on 21 May 2007.

{dagger} Supplemental material for this article may be found at http://iai.asm.org/.

Editor: F. C. Fang

Infection and Immunity, August 2007, p. 3833-3841, Vol. 75, No. 8
0019-9567/07/$08.00+0     doi:10.1128/IAI.00188-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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