S
Scott J. Hultgren
Researcher at Washington University in St. Louis
Publications - 393
Citations - 42958
Scott J. Hultgren is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Pilus & Bacterial adhesin. The author has an hindex of 109, co-authored 380 publications receiving 38674 citations. Previous affiliations of Scott J. Hultgren include University College London & Vrije Universiteit Brussel.
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Journal ArticleDOI
FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria.
Charles Hal Jones,J.S. Pinkner,A V Nicholes,Lynn N. Slonim,Soman N. Abraham,Scott J. Hultgren +5 more
TL;DR: The studies point out the general strategies used by Gram-negative bacteria to assemble adhesins into pilus fibers, allowing them to promote attachment to eukaryotic receptors, and suggest that the conserved cleft is a subunit binding feature of all members of this protein family.
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QseC-mediated dephosphorylation of QseB is required for expression of genes associated with virulence in uropathogenic Escherichia coli.
TL;DR: It is discovered that QseC has phosphatase activity required for QseB dephosphorylation, which is critical for modulatingQseB activity and subsequent gene expression, and that this is not a UPEC‐specific phenomenon.
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Design and evaluation of pilicides: potential novel antibacterial agents directed against uropathogenic Escherichia coli.
Anette Svensson,A Larsson,Hans Emtenäs,Mattias Hedenström,Tomas Fex,Scott J. Hultgren,Jerome S. Pinkner,Fredrik Almqvist,Jan Kihlberg +8 more
TL;DR: Design and evaluation of Pilicides : Potential novel antibacterial agents directed against Uropathogenic Escherichia coli and their applications in medicine and agriculture are studied.
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PapD, a periplasmic transport protein in P-pilus biogenesis.
TL;DR: It is suggested that PapD functions in P-pilus biogenesis as a periplasmic transport protein that forms complexes with pilus subunits at the outer surface of the inner membrane and transports them in a stable configuration across the periplasmsic space before delivering them to the site(s) of pilus polymerization.
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Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits.
TL;DR: It is proposed that the function of PapD and other periplasmic pilus chaperones is to partition newly translocated pilus subunits into assembly-competent complexes and thereby prevent nonproductive aggregation of the subunits in thePeriplasm.