Snapshots of usher-mediated protein secretion and ordered pilus assembly

Evan T. Saulino, Esther Bullitt, Scott J. Hultgren

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

Abstract

Type 1 pilus biogenesis was used as a paradigm to investigate ordered macromolecular assembly at the outer cell membrane. The ability of Gram-negative bacteria to secrete proteins across their outer membrane and to assemble adhesive macromolecular structures on their surface is a defining event in pathogenesis. We elucidated genetic, biochemical, and biophysical requirements for assembly of functional type 1 pili. We discovered that the minor pilus protein FimG plays a critical role in nucleating the formation of the adhesive tip fibrillum. Genetic methods were used to trap pilus subunits during their translocation through the outer membrane usher protein, providing data on the structural interactions that occur between subunit components during type 1 pilus formation. Electron microscopic and biochemical analyses of these stepwise assembly intermediates demonstrated that translocation of pilus subunits occurs linearly through the usher's central channel, with formation of the pilus helix occurring extracellularly. Specialized pilin subunits play unique roles both in this multimerization and in the final ultrastructure of the adhesive pilus.

Original languageEnglish
Pages (from-to)9240-9245
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number16
DOIs
StatePublished - Aug 1 2000

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