Genotype - phenotype
Deletion mechanism
Chromatin structure
Animal models
Positions available
Student training
Selected reading
Useful links
Contact us


Last updated:

July 2001







Facioscapulohumeral muscular dystrophy



In collaboration with Unilever Research, we implemented a novel proteomics approach to unravel the pathophysiolgical processes underlying FSHD. More precisely, we generated llama-derived phage-display immune libraries and use selected heavy-chain (VHH) antibody fragments from these libraries to study FSHD pathophysiology, both with individual antibodies in situ, as with antibody arrays. Phage-display derived VHH antibodies have characteristics that make them eminently suited for arraying purposes. They are only composed of heavy chains, which abolish the need for combining heavy and light chains, one of the major drawbacks of conventional phage-display antibodies. In general, the VHH fragments display a very high affinity and specificity for their epitopes and are extremely stable due to their single-domain character. Moreover, phage display libraries provide a rapid, inexhaustible and uniform source of antibodies. High-affinity clones can well be selected and since we have the genetic information for these antibodies, this approach is very versatile. For example, these antibodies can easily be equipped with a specific tag allowing uniform binding to pre-coated glass slides (More information: Silvère van der Maarel, Ph.D. E-mail: For job opportunities, see also  Dissecting muscle and nerve disease: functional genomics from DNA to protein

By studying protein homeostasis, including post-translational modifications, we will complement the ongoing RNA profiling studies and will thus improve our knowledge of the physiological processes that occur in FSHD. This knowledge will ultimately allow the design of new therapeutic intervention strategies.