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Volume 8, Issue 3 (Suppl)
J Clin Cell Immunol, an open access journal
ISSN: 2155-9899
Page 32
Notes:
conference
series
.com
June 29-July 01, 2017 Madrid, Spain
8
th
European
Immunology Conference
Euro Immunology 2017
June 29-July 01, 2017
Single domain antibodies for the knockdown of cytosolic and nuclear proteins
S
ingle domain antibodies (sdAbs) from camels or sharks comprise only the variable heavy chain domain. Human single
domain antibodies comprise the variable domain of the heavy chain or light chain. SdAbs are stable, non-aggregating
molecules
in vitro
and
in vivo
compared to complete antibodies and scFv fragments. They are excellent novel inhibitors of
cytosolic/nuclear proteins, because they are correctly folded inside the cytosol in contrast to scFv fragments. SdAbs are unique
because of their excellent specificity and possibility to target posttranslational modifications such as phosphorylation sites,
conformers or interaction regions of proteins that cannot be targeted with genetic knockout techniques and are impossible to
knockdown with RNAi. The most frequently selected antigenic epitopes belong to viral and oncogenic proteins, followed by
toxins, proteins of the nervous system as well as plant-and drosophila proteins. It is now possible to select functional sdAbs
against virtually every cytosolic/nuclear protein and desired epitope using synthetic single pot single domain antibody libraries
without the need of immunization. In summary, cytosolic/nuclear sdAbs of camelid, shark and human origin can be applied to
clarify the function of uncharacterized proteins such as virus proteins and host cell factors, oncogenic proteins and cofactors,
proteins of the nervous system, intracellular enzymes involved in signaling, transcription factors and proteins involved in
differentiation and development.
Biography
Thomas Böldicke has obtained his PhD degree fromMax Planck Institute of Molecular Genetics, Berlin. Since 1986, he has been working at Helmholtz Centre for Infection
Research, as a Project Leader of Intracellular Antibodies.
thomas.boeldicke@helmholtz-hzi.deThomas Böldicke
Helmholtz Centre for Infection Research, Germany
Thomas Böldicke, J Clin Cell Immunol 2017, 8:3(Suppl)
DOI: 10.4172/2155-9899-C1-035