The Journal of Experimental Medicine
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Published online 8 November 2004 doi:10.1084/jem.20040500
Rockefeller University Press, 0022-1007 $8.00
JEM, Volume 200, Number 10, 1267-1278
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Bartonella Adhesin A Mediates a Proangiogenic Host Cell Response

Tanja Riess1, Siv G.E. Andersson4, Andrei Lupas5, Martin Schaller2, Andrea Schäfer1, Pierre Kyme1, Jörg Martin5, Joo-Hee Wälzlein1, Urs Ehehalt1, Hillevi Lindroos4, Markus Schirle3, Alfred Nordheim3, Ingo B. Autenrieth1, and Volkhard A.J. Kempf1

1 Institut für Medizinische Mikrobiologie und Hygiene, Department of Molecular Biology, Eberhard-Karls-Universität, 72076 Tübingen, Germany
2 Universitäts-Hautklinik, Department of Molecular Biology, Eberhard-Karls-Universität, 72076 Tübingen, Germany
3 Institute for Cell Biology, Department of Molecular Biology, Eberhard-Karls-Universität, 72076 Tübingen, Germany
4 Department of Molecular Evolution, Evolutionary Biology Center, Uppsala University, 75236 Uppsala, Sweden
5 Max-Planck-Institut für Entwicklungsbiologie, 72076 Tübingen, Germany

Address correspondence to Volkhard A.J. Kempf, Institut für Medizinische Mikrobiologie und Hygiene, Eberhard-Karls-Universität, Elfriede-Aulhorn-Strasse 6, 72076 Tübingen, Germany. Phone: 49-7071-2981526; Fax: 49-7071-295440; email: volkhard.kempf{at}med.uni-tuebingen.de

Bartonella henselae causes vasculoproliferative disorders in humans. We identified a nonfimbrial adhesin of B. henselae designated as Bartonella adhesin A (BadA). BadA is a 340-kD outer membrane protein encoded by the 9.3-kb badA gene. It has a modular structure and contains domains homologous to the Yersinia enterocolitica nonfimbrial adhesin (Yersinia adhesin A). Expression of BadA was restored in a BadA-deficient transposon mutant by complementation in trans. BadA mediates the binding of B. henselae to extracellular matrix proteins and to endothelial cells, possibly via ß1 integrins, but prevents phagocytosis. Expression of BadA is crucial for activation of hypoxia-inducible factor 1 in host cells by B. henselae and secretion of proangiogenic cytokines (e.g., vascular endothelial growth factor). BadA is immunodominant in B. henselae–infected patients and rodents, indicating that it is expressed during Bartonella infections. Our results suggest that BadA, the largest characterized bacterial protein thus far, is a major pathogenicity factor of B. henselae with a potential role in the induction of vasculoproliferative disorders.

Key Words: pilus • endothelial cells • HIF-1 • VEGF • angiogenesis

P. Kyme's present address is Centre for Infectious Diseases and Microbiology, University of Sydney, Westmead Hospital, New South Wales 2145, Australia.

Abbreviations used in this paper: ADM, adrenomedullin; BA, bacillary angiomatosis; BadA, Bartonella adhesin A; BP, bacillary peliosis; CBA, Columbia blood agar; CLSM, confocal laser scanning microscopy; CSD, cat scratch disease; EC, endothelial cell; ECM, extracellular matrix; Fn, fibronectin; HIF, hypoxia-inducible factor; HMW, high molecular weight; IEM, immunoelectronmicroscopy; IGFBP-3, insulin-like growth factor binding protein 3; NadA, Neisseria adhesin A; OMP, outer membrane protein; PFA, paraformaldehyde; TEM, transmission electron microscopy; VEGF, vasculoendothelial growth factor; YadA, Yersinia adhesin A.


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