Diagnostic Microbiology & Infectious Disease
Volume 55, Issue 1 , Pages 1-7, May 2006

Production of recombinant Bartonella henselae 17-kDa protein for antibody-capture enzyme-linked immunosorbent assay

Portions of this study were presented at the 105th General Meeting of the American Society for Microbiology, Atlanta, GA, June 2005.

Department of Research and Development, Medical Diagnostic Laboratories, L.L.C., Hamilton, NJ 08690, USA

Received 29 June 2005; received in revised form 19 October 2005; accepted 26 October 2005.

Abstract 

The Bartonella henselae 17-kDa protein was expressed in a prokaryotic expression system as a histidine-tagged fusion protein and was purified. The target gene was cloned into a recombinant expression construct, pTri-17kd. The expressed protein was purified to near homogeneity by a nickel-agarose column chromatography. Protein recovery was estimated to be 2.9 mg from 100 mL of bacterial culture. The purified 17-kDa protein was recognized by serum from patients infected with B. henselae and Bartonella quintana, suggesting antigenic integrity. The sensitivity and specificity of the IgG enzyme-linked immunosorbent assay (ELISA) relative to immunofluorescent antibody assay testing were 71.1% and 93.0%, respectively. According to the receiver operating characteristic curve analysis, the area under the curve was 0.823. These results indicate that the expressed 17-kDa protein is a suitable source of antigen for development of an antibody-capture ELISA for the detection of antibodies to B. henselae.

Keywords: Bartonella, 17-kDa protein, ELISA, Cat scratch disease

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PII: S0732-8893(05)00347-0

doi:10.1016/j.diagmicrobio.2005.10.020

Diagnostic Microbiology & Infectious Disease
Volume 55, Issue 1 , Pages 1-7, May 2006

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