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Bartonella adhesin A mediates a proangiogenic host cell response
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Evolution, Genomics and Systematics, Molecular Evolution.
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2004 (English)In: Journal of Experimental Medicine, ISSN 0022-1007, E-ISSN 1540-9538, Vol. 200, no 10, 1267-1278 p.Article in journal (Refereed) Published
Abstract [en]

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 β1 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.

Place, publisher, year, edition, pages
2004. Vol. 200, no 10, 1267-1278 p.
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Biological Sciences
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URN: urn:nbn:se:uu:diva-70779DOI: 10.1084/jem.20040500OAI: oai:DiVA.org:uu-70779DiVA: diva2:98690
Available from: 2005-04-28 Created: 2005-04-28 Last updated: 2017-11-21Bibliographically approved

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Andersson, SivLindroos, Hillevi

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