We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
The head of Bartonella adhesin A is crucial for host cell interaction of Bartonella henselae.
- Authors
Kaiser, Patrick O.; Riess, Tanja; Wagner, Carola L.; Linke, Dirk; Lupas, Andrei N.; Schwarz, Heinz; Raddatz, Günter; Schäfer, Andrea; Kempf, Volkhard A. J.
- 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.
- Subjects
BARTONELLA; BARTONELLACEAE; HYPOXEMIA; INFLUENCE of altitude; PHYSIOLOGICAL effects of oxygen; VASCULAR grafts; EXTRACELLULAR matrix proteins; CELL communication; CELLULAR control mechanisms
- Publication
Cellular Microbiology, 2008, Vol 10, Issue 11, p2223
- ISSN
1462-5814
- Publication type
Article
- DOI
10.1111/j.1462-5822.2008.01201.x