Han Remaut Lab

Research focus

​Work in our group focuses on the structural molecular biology of bacterial cell surfaces & host-pathogen interactions. For most pathogenic bacteria, a crucial initial step in the establishment of infection is the recognition and colonization of the host tissue by specific attachment via surface-exposed adhesion molecules. In gram-negative bacteria, these adhesins are displayed on the outer membrane as single proteins (e.g. autotransporters or two-partner secretion systems) or can be incorporated into filamentous polymers (chaperone/usher pili, type II pili, type IV secretion pili and curli). Adhesin-mediated attachment can simply serve as a means of avoiding clearance through mechanical shear, or can trigger more complex host responses like cytoskeleton reorganization and cell invasion, or provide the required proximity to the host cell to enable other virulence mechanisms to come into action (e.g. effector injection through type III and type IV secretion systems).
 In an era of increased antibiotics resistance and difficulties in controlling hospital-acquired infections, it is essential to gain a better understanding of the fundamental principles governing the infection process. Our lab studies the structural molecular biology of bacterial adhesins and cell-surface filaments with respect to their function in bacterial pathogenesis, with the ultimate aim of developing a new generation of virulence-targeted antimicrobials.

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. Mounting evidence shows that the presence of only a selected number of virulence factors is associated with disease-causing HP strains, responsible for peptic ulceration and an increased risk for gastric cancers. 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 fibers

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), respectively. They are assembled by the conserved chaperone/usher (CU) pathway, responsible for the biogenesis of more than 100 surface organelles in many other important human pathogens (including Yersinia, Salmonella, Shigella, Haemophilus). Two strategies are investigated for countering pilus-mediated disease processes: (1) anti-adhesive compounds targeted against the adhesive sub-units (2) pilus biogenesis inhibitors.

Curli - Structural biology of controlled amyloid deposition

Curli are proteinaceous filaments found on the surfaces of E. coli and Salmonella species where they mediate biofilm formation and have been shown to bind a range of human plasma and contact-phase proteins. Curli fibers exhibit typical characteristics of amyloids. 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 sub-unit 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.​


Nucleation and growth of a bacterial functional amyloid at single-fiber resolutionSleutel M* Van Den Broeck I* Van Gerven N* Feuillie C Jonckheere W Valotteau C Dufrene Y Remaut HNature Chemical Biology, 13, 902-908, 2017* or °: authors contributed equally
Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pyloriMoonens K* Gideonsson P* Subedi S Bugaytsova J Romao E Mendez M Norden J Fallah M Rakhimova L Shevtsova A Lahmann M Castaldo G Brannstrom K Coppens F Lo A Ny T Solnick J Vandenbussche G Oscarson S Hammarstrom L Arnqvist A Berg D Muyldermans S Boren T* Remaut H*Cell Host & Microbe, 19, 55-66, 2016* or °: authors contributed equally
Inflammation-Induced Adhesin-Receptor Interaction Provides a Fitness Advantage to Uropathogenic E. coli during Chronic InfectionConover M* Ruer S* Taganna J Kalas V De Greve H Pinkner J Dodson K Remaut H* Hultgren S*Cell Host & Microbe, 20, 482-492, 2016* or °: authors contributed equally
Bacterial Amyloid Formation: Structural Insights into Curli BiogensisVan Gerven Nani Klein R Hultgren S. Remaut HanTRENDS IN MICROBIOLOGY, 23, 693-706, 2015
Structural and mechanistic insights into the bacterial amyloid secretion channel CsgGGoyal Parveen Krasteva P. V Van Gerven Nani Gubellini F Van den Broeck Imke Troupiotis-Tsailaki A Jonckheere Wim Pehau-Arnaudet G Pinkner J Chapman M. S Hultgren S. Howorka S Fronzes R. Remaut HanNATURE, 516, 250-3, 2014

Job openings


Stripping down bacterial armor: a new way to fight anthrax

15/07/2019 - A new study led by Antonella Fioravanti in the lab of Han Remaut (VIB-VUB Center for Structural Biology) has shown that removing the armor of the bacterium that causes anthrax slows its growth and negatively affects its ability to cause disease.

Research center for high-resolution electron cryogenic microscopy to open

21/09/2018 - The Center for Structural Biology (VIB-VUB), headed by Professors Jan Steyaert and Han Remaut officially opened the ‘international facility for Bio Electron Cryogenic Microscopy’ (BECM) at the VUB Campus in Brussels.

Researchers gain new insights into the formation of non-pathological amyloids

19/06/2017 - The team of Han Remaut and the lab of Yves Dufrêne at UCL Louvain-La-Neuve collaborated on a study of functional amyloids –protein aggregates with typical amyloid structure that do not lead to disease but rather serve a dedicated biological function.

New receptors discovered for stomach germ Helicobacter pylori

18/10/2016 - Research groups of the Technical University of Munich, the University of Duisburg-Essen and VIB–VUB has discovered a completely new approach to preventing or treating infections with this bacterium as well as secondary complications.

Researchers take a new step towards non-antibiotic bladder infection therapies

23/09/2016 - A team of scientists has gained fresh insight into the development of bladder infections, also known as cystitis. These findings are the result of VIB-VUB researchers & their American colleagues at the center for Women’s Infectious Disease Research.

VIB science in groundbreaking DNA sequencing technology

23/07/2016 - ​A collaboration between VIB and Oxford Nanopore Technologies has led to the development of a new key element of state-of-the-art DNA sequencing tools. The lab of Han Remaut conducted groundbreaking research on a pore protein.

New insights into H. Pylori unmask a 'molecular chameleon'

06/05/2016 - ​The bacterium ‘Helicobacter pylori’ is highly adapted to survival in the human stomach and is responsible for the majority of gastric ulcer and cancer cases worldwide. Scientists at the lab of Han Remaut (VIB/VUB) present new insights into BabA.

VIB announces collaboration with Oxford Nanopore Technologies on new DNA sequencing nanopore

08/03/2016 - ​VIB is proud to announce that the lab of Han Remaut (VIB/Vrije Universiteit Brussels) has teamed up with Oxford Nanopore Technologies for the development of nanopore sensing technology.

Novel insights in the attachment of the bacterial carcinogen Helicobacter pylori

14/01/2016 - This BabA protein proves to be a molecular chameleon that adapts it binding properties and preference for different ABO-blood group sugars according to their prevalence in different human populations.

New insights into bacterial protein secretion

13/02/2015 - Using X-ray crystallography, Parveen Goyal and Han Remaut (VIB/Vrije Universiteit Brussel) created a detailed three-dimensional image of the pores through which the curli building blocks cross the bacterial cell envelope.

VIB scientists find new strategy to combat bacterial infections

29/01/2014 - Alvin Lo and Han Remaut (VIB/Vrije Universiteit Brussel) have identified a chemical substance with the potential of acting as a new drug to treat bacterial infections, particularly urinary tract infections.

Han Remaut

Han Remaut

Research area(s)

Model organism(s)


​​PhD: Ghent University, Ghent, Belgium, 2003
Postdoc.: Inst. for Structural Molecular Biology, School of Crystallography, Birkbeck College, UK, 2003-08
VIB Group leader since 2009
VIB Science Director since 2017

Contact Info

VIB-VUB Center for Structural BiologyBuilding EPleinlaan 2 1050 BRUSSELRoute description