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CagL is an essential pilus surface component of the virulence‐associated type IV secretion system (T4SS) employed by Helicobacter pylori to translocate the oncogenic effector protein CagA into human gastric epithelial cells. CagL contains an RGD motif and integrin α5β1 is widely accepted as its host cell receptor. Here, we show that CagL binds integrin αVβ6 with substantially higher affinity and that...
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