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Adhesins of Bartonella spp.

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Bacterial Adhesion

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 715))

Abstract

Adhesion to host cells represents the first step in the infection process and one of the decisive features in the pathogenicity of Bartonella spp. B. henselae and B. quintana are considered to be the most important human pathogenic species, responsible for cat scratch disease, bacillary angiomatosis, trench fever and other diseases. The ability to cause vasculoproliferative disorders and intraerythrocytic bacteraemia are unique features of the genus Bartonella. Consequently, the interaction with endothelial cells and erythrocytes is a focus in Bartonella research. The genus harbours a variety of trimeric autotransporter adhesins (TAAs) such as the Bartonella adhesin A (BadA) of B. henselae and the variably expressed outer-membrane proteins (Vomps) of B. quintana, which display remarkable variations in length and modular construction. These adhesins mediate many of the biologically-important properties of Bartonella spp. such as adherence to endothelial cells and extracellular matrix proteins and induction of angiogenic gene programming. There is also significant evidence that the laterally acquired Trw-conjugation systems of Bartonella spp. mediate host-specific adherence to erythrocytes. Other potential adhesins are the filamentous haemagglutinins and several outer membrane proteins. The exact molecular functions of these adhesins and their interplay with other pathogenicity factors (e.g., the VirB/D4 type 4 secretion system) need to be analysed in detail to understand how these pathogens adapt to their mammalian hosts.

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Acknowledgments

Parts of this manuscript have been reprinted in a modified form from “Kaiser, P.O., Riess, T., O’Rourke, F., Linke, D., and Kempf, V.A. (2011). Bartonella spp.: throwing light on uncommon human infections. Int J Med Microbiol 301: 7–15”.

The work of V. Kempf is supported by grants from the Deutsche Forschungsgemeinschaft (DFG). We thank Heinz Schwarz and Jürgen Berger (Max Planck-Institut Tübingen, Germany) for providing electron microscopy of B. henselae.

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Authors and Affiliations

  1. Institut für Medizinische Mikrobiologie und Krankenhaushygiene, Universitätsklinikum, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany

    Fiona O’Rourke, Thomas Schmidgen & Patrick O. Kaiser

  2. Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany

    Dirk Linke

  3. Institut für Medizinische Mikrobiologie und Krankenhaushygiene, Universitätsklinikum, Johann Wolfgang Goethe-Universität, 60596, Frankfurt am Main, Germany

    Volkhard A.J. Kempf

Authors
  1. Fiona O’Rourke
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  2. Thomas Schmidgen
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  3. Patrick O. Kaiser
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  4. Dirk Linke
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  5. Volkhard A.J. Kempf
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Corresponding author

Correspondence to Volkhard A.J. Kempf .

Editor information

Editors and Affiliations

  1. , Department I, Protein Evolution, Max-Planck Institute for Developmental B, Spemannstr. 35, Tübingen, 72076, Germany

    Dirk Linke

  2. , Institute of Biotechnology, University of Helsinki, Viikinkaari 1, Helsinki, FIN-00014, Finland

    Adrian Goldman

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© 2011 Springer Science+Business Media B.V.

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O’Rourke, F., Schmidgen, T., Kaiser, P.O., Linke, D., Kempf, V.A. (2011). Adhesins of Bartonella spp.. In: Linke, D., Goldman, A. (eds) Bacterial Adhesion. Advances in Experimental Medicine and Biology, vol 715. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-0940-9_4

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