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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: /CMR
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