H
Han Remaut
Researcher at Vrije Universiteit Brussel
Publications - 110
Citations - 5278
Han Remaut is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Bacterial outer membrane & Pilus. The author has an hindex of 36, co-authored 100 publications receiving 4388 citations. Previous affiliations of Han Remaut include Technische Universität München & Free University of Brussels.
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Journal ArticleDOI
Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria
Jerome S. Pinkner,Han Remaut,Floris Buelens,Eric L. Miller,Veronica Åberg,Nils Pemberton,Mattias Hedenström,Andreas Larsson,Patrick C. Seed,Gabriel Waksman,Scott J. Hultgren,Fredrik Almqvist +11 more
TL;DR: These pilicides target key virulence Factors in pathogenic bacteria and represent a promising proof of concept for developing drugs that function by targeting virulence factors.
Journal ArticleDOI
Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG
Parveen Goyal,Petya V. Krasteva,Nani Van Gerven,Francesca Gubellini,Imke Van den Broeck,Anastassia Troupiotis-Tsaïlaki,Wim Jonckheere,Gérard Pehau-Arnaudet,Jerome S. Pinkner,Matthew George Chapman,Scott J. Hultgren,Stefan Howorka,Rémi Fronzes,Han Remaut +13 more
TL;DR: Structural, functional and electrophysiological analyses imply that Escherichia coli CsgG is an ungated, non-selective protein secretion channel that is expected to employ a diffusion-based, entropy-driven transport mechanism.
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Fiber formation across the bacterial outer membrane by the chaperone/usher pathway.
Han Remaut,Chunyan Tang,Nadine S. Henderson,Jerome S. Pinkner,Tao Wang,Scott J. Hultgren,David G. Thanassi,Gabriel Waksman,Huilin Li,Huilin Li +9 more
TL;DR: The structural basis for pilus fiber assembly and secretion performed by the outer membrane assembly platform--the usher--is revealed by the crystal structure of the translocation domain of the P pilus usher PapC and single particle cryo-electron microscopy imaging of the FimD usher bound to a translocating type 1 pilus assembly intermediate.
Journal ArticleDOI
Fiber assembly by the chaperone–usher pathway
TL;DR: Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence, which releases folding energy that drives subunit incorporation into the fiber, which grows through a pore formed by the outer-membrane usher.
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Selective depletion of uropathogenic E. coli from the gut by a FimH antagonist
Caitlin N. Spaulding,Roger D. Klein,Ségolène Ruer,Andrew L. Kau,Henry L. Schreiber,Zachary T. Cusumano,Karen W. Dodson,Jerome S. Pinkner,Daved H. Fremont,James W. Janetka,Han Remaut,Jeffrey I. Gordon,Scott J. Hultgren +12 more
TL;DR: It is shown that F17-like and type 1 pili promote intestinal colonization and show distinct binding to epithelial cells distributed along colonic crypts, and targeting FimH with M4284, a high-affinity inhibitory mannoside, reduces intestinal colonization of genetically diverse UPEC isolates, while simultaneously treating UTI, without notably disrupting the structural configuration of the gut microbiota.