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: email@example.com).
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muscle and nerve disease: functional genomics from DNA to protein”
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.