title: Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion.
abstract: Two-partner secretion (TPS) is the most widely distributed secretion pathway known. These systems export large exoproteins through highly conserved channel-forming beta-barrel proteins. Filamentous haemagglutinin (FHA), expressed by Bordetella species, is the prototypical TPS family member. Here we show that the C-terminus of mature FHA, as opposed to the N-terminus as previously proposed, is exposed on the cell surface and is required for mediating adherence to cultured epithelial cells. We show that the C-terminus of the FHA pro-protein (FhaB) is required for FHA function in vitro and in vivo and we show that cleavage of FhaB to form FHA is not the mechanism by which FHA is released from the cell. Based on these data, we propose a new model for TPS. This model provides an explanation for the energetics of export of globular protein domains across membranes in the absence of ATP and it suggests a new mechanism for the control of protein folding.
authors.affiliation: Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-9610, USA.
authors.forename: Joseph
authors.initials: J
authors.lastname: Mazar
authors.forename: Peggy A
authors.initials: PA
authors.lastname: Cotter
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D001422:Bacterial Adhesion / Q000502:physiology; D001426:Bacterial Proteins / Q000378:metabolism; D016950:Bordetella bronchiseptica / Q000378:metabolism*; D001886:Bordetella pertussis / Q000378:metabolism*; D002478:Cells, Cultured; D004847:Epithelial Cells / Q000382:microbiology; D008168:Lung / Q000166:cytology / Q000382:microbiology; D010446:Peptide Fragments / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D051381:Rats; D017208:Rats, Wistar; D012697:Serine Endopeptidases / Q000378:metabolism; D010566:Virulence Factors, Bordetella / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D010446:Peptide Fragments; D011498:Protein Precursors; D010566:Virulence Factors, Bordetella; C065273:filamentous hemagglutinin adhesin, Bordetella pertussis; D012697:Serine Endopeptidases; C437318:SphB1 protein, Bordetella pertussis