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  The head of Bartonella adhesin A is crucial for host cell interaction of Bartonella henselae

Kaiser, P., Riess, T., Wagner, C., Linke, K., Lupas, A., Schwarz h, H., et al. (2008). The head of Bartonella adhesin A is crucial for host cell interaction of Bartonella henselae. Cellular Microbiology, 10(11), 2223-2234. doi:10.1111/j.1462-5822.2008.01201.x.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-2CA1-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-2CA2-5
Genre: Journal Article

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 Creators:
Kaiser, PO, Author
Riess, T, Author
Wagner, CL, Author
Linke, K, Author
Lupas, AN1, Author
Schwarz h, H1, Author
Raddatz, G2, 3, Author              
Schäfer, A, Author
Kempf, VAJ, Author
Affiliations:
1Max Planck Institute for Developmental Biology, Max Planck Society, Max-Planck-Ring 5, 72076 Tübingen, DE, ou_2421691              
2Former Department MRZ, Max Planck Institute for Biological Cybernetics, Max Planck Society, ou_2528700              
3Max Planck Institute for Biological Cybernetics, Max Planck Society, Spemannstrasse 38, 72076 Tübingen, DE, ou_1497794              

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 Abstract: Human pathogenic Bartonella henselae cause cat scratch disease and vasculoproliferative disorders (e.g. bacillary angiomatosis). Expression of Bartonella adhesin A (BadA) is crucial for bacterial autoagglutination, adhesion to host cells, binding to extracellular matrix proteins and proangiogenic reprogramming via activation of hypoxia inducible factor (HIF)‐1. Like the prototypic Yersinia adhesin A, BadA belongs to the class of trimeric autotransporter adhesins and is constructed modularly consisting of a head, a long and repetitive neck‐stalk module and a membrane anchor. Until now, the exact biological role of these domains is not known. Here, we analysed the function of the BadA head by truncating the repetitive neck‐stalk module of BadA (B. henselae badA–/pHN23). Like B. henselae Marseille wild type, B. henselae badA–/pHN23 showed autoagglutination, adhesion to collagen and endothelial cells and activation of HIF‐1 in host cells. Remarkably, B. henselae badA–/pHN23 did not bind to fibronectin (Fn) suggesting a crucial role of the deleted stalk domain in Fn binding. Additionally, the recombinantly expressed BadA head adhered to human umbilical vein endothelial cells and to a lesser degree to epithelial (HeLa 229) cells. Our data suggest that the head represents the major functional domain of BadA responsible for host adhesion and angiogenic reprogramming.

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 Dates: 2008-11
 Publication Status: Published in print
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 Rev. Method: -
 Identifiers: DOI: 10.1111/j.1462-5822.2008.01201.x
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Title: Cellular Microbiology
Source Genre: Journal
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Publ. Info: Malden, MA : Blackwell Science
Pages: - Volume / Issue: 10 (11) Sequence Number: - Start / End Page: 2223 - 2234 Identifier: ISSN: 1462-5814
CoNE: https://pure.mpg.de/cone/journals/resource/959328105032