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Han Remaut

  • PhD: Ghent University, Ghent, Belgium, Feb. 2003
  • Postdoc: Institute of Structural Molecular Biology, Birkbeck College, London - UK, '03-'08
  • Odysseus Fellow & VIB Group Leader from Jan. 2009


Helicobacter pylori Adhesion - Countering a Life-long Attachment to the Host

Due to its extreme persistence in the host and the known involvement of a complex adherence profile in maintaining infection,Helicobacter forms the ideal proof-of-principle case for the development of anti-adhesin drugs. In addition, mounting evidence shows that the presence of only a selected number of virulence factors is associated with disease-causing HP strains. Indeed, only ~10% of HP infected individuals will ever develop clinical disease. The development of anti-virulence therapies targeting HP adhesins has the potential for the broad-scale selective clearance of pathogenic HP strains only.

Chaperone/Usher Pilus Assembly - Towards Selective Disarmament of Adhesive Fibres

P and type 1 pili are responsible for the early onset and persistence of UPEC-caused urinary tract infections (UTIs) by mediating attachment to the kidney epithelium (P pili) or attachment and invasion of the bladder epithelium cells (type 1 pili). They are assembled by the conserved chaperone/usher (CU) pathway, responsible for the biogenesis of over a 100 surface organelles in many other important human pathogens (including Yersinia, Salmonella, Shigella, Haemophilus).Based on our detailed structural and functional characterization of the CU assembly pathway, we will develop subunit recruitment and polymerizations inhibitors, which could potentially serve as generic CU organelle biogenesis inhibitors.


Curli - Structural of Biology of Controlled Amyloid Deposition

Curli are proteinaceous filaments found on the surfaces of E. coli and Salmonella species that mediate biofilm formation and have been shown to bind a range of human plasma and contact-phase proteins. Curli fibers exhibit typical characteristics of amyloid and are extremely stable and highly resistant to depolymerization. Contrary to what is seen in human pathogenic amyloid depositions, curli formation follows a controlled biosynthetic pathway involving several protein co-factors that prevent premature aggregation and guide subunit passage through the bacterial periplasm and outer membrane. We study the structural molecular biology of curli biosynthesis as a model system for controlled amyloid deposition and as a route towards future nanobiotechnological applications.


Selected Publications:

Fronzes R, Remaut H, Waksman G. Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria. EMBO J 27, 2271-80, 2008

Remaut H, Tang C, Henderson N, Pinkner J, Wang T, Hultgren S, Thanassi D, Waksman G, Li H. Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. CELL 133, 640-52, 2008

Pinkner J, Remaut H, Buelens F, Miller E, Aberg V, Pemberton N, Hedenstrom M, Larsson A, Seed P, Waksman G, Hultgren S, Almqvist F. Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria. P NATL ACAD SCI USA 103, 17897-902, 2006

Remaut H, Rose R, Hannan T, Hultgren S, Radford S, Ashcroft A, Waksman G. Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. MOL CELL 22, 831-42, 2006

Remaut H, Waksman G. Structural biology of bacterial pathogenesis. CURR OPIN STRUC BIOL 14, 161-70, 2004




Dr. Han Remaut



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