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Updated: Jan 27, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Bordetella Filamentous Hemagglutinin, a Model for the Two-Partner Secretion Pathway
Zachary M Nash1, Peggy A Cotter1
1Department of Microbiology and Immunology, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599.
Abstract:
Bacteria use a variety of mechanisms to translocate proteins from the cytoplasm, where they are synthesized, to the cell surface or extracellular environment or directly into other cells, where they perform their ultimate functions. Type V secretion systems (T5SS) use β-barrel transporter domains to export passenger domains across the outer membranes of Gram-negative bacteria. Distinct among T5SS are type Vb or two-partner secretion (TPS) systems in which the transporter and passenger are separate proteins, necessitating a mechanism for passenger-translocator recognition in the periplasm and providing the potential for reuse of the translocator. This review describes current knowledge of the TPS translocation mechanism, using Bordetella filamentous hemagglutinin (FHA) and its transporter FhaC as a model. We present the hypothesis that the TPS pathway may be a general mechanism for contact-dependent delivery of toxins to target cells.
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