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Infection and Immunity, November 2007, p. 5255-5263, Vol. 75, No. 11
0019-9567/07/$08.00+0     doi:10.1128/IAI.00533-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Characterization of an Immunogenic Outer Membrane Autotransporter Protein, Arp, of Bartonella henselae

Section of Clinical Immunology, Microbiology and Virology, Department of Pathology, University of Utah, Salt Lake City, Utah 84132,¹ Associated Regional and University Pathologists (ARUP) Institute for Clinical and Experimental Pathology, Salt Lake City, Utah 84108²

Received 13 April 2007/ Returned for modification 20 May 2007/ Accepted 23 August 2007

Bartonella henselae is a recently recognized pathogenic bacterium associated with cat scratch disease, bacillary angiomatosis, and bacillary peliosis. This study describes the cloning, sequencing, and characterization of an antigenic autotransporter gene from B. henselae. A cloned 6.0-kb BclI-EcoRI DNA fragment expresses a 120-kDa B. henselae protein immunoreactive with 21.2% of sera from patients positive for B. henselae immunoglobulin G antibodies by indirect immunofluorescence, with 97.3% specificity and no cross-reactivity with antibodies against various other organisms. DNA sequencing of the clone revealed one open reading frame of 4,320 bp with a deduced amino acid sequence that shows homology to the family of autotransporters. The autotransporters are a group of proteins that mediate their own export through the outer membrane and consist of a passenger region, the -domain, and an outer membrane transporter region, the ß-domain. The passenger domain shows homology to a family of pertactin-like adhesion proteins and contains seven, nearly identical 48-amino-acid repeats not found in any other bacterial or Bartonella DNA sequences. The passenger -domain has a calculated molecular mass of 117 kDa, and the transporter ß-domain has a calculated molecular mass of 36 kDa. The clone expresses a 120-kDa protein and a protein that migrates at approximately 38 kDa exclusively in the outer membrane protein fraction, suggesting that the 120-kDa passenger protein remains associated with the outer membrane after cleavage from the 36-kDa transporter.

Published ahead of print on 4 September 2007.

Editor: A. Camilli