BadA, a trimeric autotransporter adhesin of B. henselae.

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BadA, a trimeric autotransporter adhesin of B. henselae. BadA, a trimeric autotransporter adhesin of B. henselae. Left, the different virulence phenotypes that have been attributed to BadA in experiments with the B. henselae Marseille strain are summarized in a schematic drawing. Note that a direct or indirect causal relationship between the attachment to β1-integrins and the activation of HIF-1/2 or NF-κB seems likely but has not been demonstrated. Right, transmission electron micrographs of wild-type B. henselae Marseille and a mutant lacking BadA expression. Not only is the remarkable size of the trimeric autotransporter adhesin obvious (bar, ca. 240 nm), but a close view also reveals spots of electron density that may be the head domains (arrow). (Right panels adapted from reference 306 with permission.)‏ Alexander Harms, and Christoph Dehio Clin. Microbiol. Rev. 2012; doi:10.1128/CMR.05009-11