3d9x
Structure of the head of the Bartonella adhesin BadAStructure of the head of the Bartonella adhesin BadA
Structural highlights
FunctionBADA_BARHN Mediates bacterial adherence to host endothelial cells and host extracellular matrix proteins (collagen type I, III, IV, laminin and fibronectin). Static versus dynamic adherence results differ slightly; in dynamic adherence studies bacteria bind to fixed components under a constant defined flow rate to simulate in vivo infection conditions (PubMed:15534369, PubMed:17060468, PubMed:18627378, PubMed:21536788, PubMed:23163798). Induces secretion of host proangiogenic cytokines such as VEGFA, ADM, IGFBP-3 and IL-8. May prevent bacterial phagocytosis by macrophages (PubMed:15534369) (Probable). Probably mediates bacterial autoagglutination (PubMed:17060468, PubMed:18627378). Negatively impacts type IV secretion system effectors (VirB/D4 T4SS and its substrate Bep proteins), possibly by preventing close association of host and bacterial cells. This implies the 2 factors are expressed at different times during infection (Probable).[1] [2] [3] [4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTrimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and presumably represent a general solution to the problem of adhesion in proteobacteria. The general structure of TAAs follows a head-stalk-anchor architecture, where the heads are the primary mediators of attachment and autoagglutination. In the major adhesin of Bartonella henselae, BadA, the head consists of three domains, the N-terminal of which shows strong sequence similarity to the head of Yersinia YadA. The two other domains were not recognizably similar to any protein of known structure. We therefore determined their crystal structure to a resolution of 1.1 A. Both domains are beta-prisms, the N-terminal one formed by interleaved, five-stranded beta-meanders parallel to the trimer axis and the C-terminal one by five-stranded beta-meanders orthogonal to the axis. Despite the absence of statistically significant sequence similarity, the two domains are structurally similar to domains from Haemophilus Hia, albeit in permuted order. Thus, the BadA head appears to be a chimera of domains seen in two other TAAs, YadA and Hia, highlighting the combinatorial evolutionary strategy taken by pathogens. Structure of the head of the Bartonella adhesin BadA.,Szczesny P, Linke D, Ursinus A, Bar K, Schwarz H, Riess TM, Kempf VA, Lupas AN, Martin J, Zeth K PLoS Pathog. 2008 Aug 8;4(8):e1000119. PMID:18688279[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||