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註釋Pathogenic Escherichia coli strains use two separate but closely related systems to export important virulence factors. The type 2 secretion (T2S) and type IV pilus (T4P) systems have considerable structural homology; both contain an outer membrane secretin complex, a pilus structure, and an inner membrane subassembly complex. The pilus structure, which predominantly consists of a major pilin subunit, is assembled from individual monomers, although this process remains poorly understood. However, the exported products are different. The T2S secretes fully folded exoproteins like heat-labile toxin through the outer membrane. In this case a pseudopilus structure is proposed to act as a piston to push the substrate through the outer membrane pore. In contrast, the T4P substrate is the pilus itself, and is used by the bacterium for aggregation and attachment to host cells.