Fiber assembly by the chaperone-usher pathway.
Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence. The periplasmic chaperone facilitates the initial folding of fiber subunits but then traps them in activated folding transition states. Chaperone dissociation releases the folding energy that drives subunit incorporation into the fiber, which grows through a pore formed by the outer-membrane usher.
Sauer
Frederic G
FG
Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Ave., New Haven, CT 06536, USA.
Remaut
Han
H
Hultgren
Scott J
SJ
Waksman
Gabriel
G
D001426:Bacterial Proteins / Q000502:physiology*; D036781:Fimbriae Proteins / Q000378:metabolism* / Q000502:physiology; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000502:physiology*; D018832:Molecular Chaperones / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation
D001426:Bacterial Proteins; D018832:Molecular Chaperones; D036781:Fimbriae Proteins