Seminar: Prof. Hidde Ploegh

Imaging immunity: antibody fragments and their enzymatic modification

Date:
3 June 2015 10:00 hrs. - 11:00 hrs.
Location:
Location see remarks
Title:
Imaging immunity: antibody fragments and their enzymatic modification
Speaker(s):

Prof. Hidde Ploegh, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, USA.

Host(s):

Dr. Martijn Verdoes, Dept. of Tumor Immunology, RIMLS

03-06-2015 10:00:0003-06-2015 11:00:00Europe/AmsterdamImaging immunity: antibody fragments and their enzymatic modification Location see remarksRimlsrimls@radboudumc.nl

Remarks / more information:

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Location: OOV: NIG Building, route 448 (-2)

Antibodies are indispensable tools to diagnose the presence of immune cells and for manipulating their function. They serve as therapeutic agents as well, especially in the treatment of cancer.  Different antibody formats may be required for optimal performance in each application. My laboratory has begun to generate single domain antibody fragments (VHHs) derived from camelid heavy chain-only antibodies for three principal reasons. First, they can be expressed in the cytosol of mammalian cells with retention of antigen binding properties, thus enabling perturbation of protein-protein interactions in the context of phenotypic screens. Second, they serve as crystallization chaperones that can assist in structure determination and thus provide the molecular link between the epitope targeted, and the phenotypic consequences of occlusion of the epitope recognized by these VHHs. Third, the small size of VHHs lends itself to a large number of genetic, enzymatic and chemical transformations that can turn VHHs into diagnostic and therapeutic agents.  We have made extensive use of a sortase-catalyzed transformation to equip both full-sized antibodies and VHHs with modifications of choice.  

Key Publications

  • Noninvasive imaging of immune responses. Proc Natl Acad Sci U S A. 112: 6146-51, 2015.
  • Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor. Science. 347: 1113-7, 2015. 
  • Intracellular expression of camelid single-domain antibodies specific for influenza virus nucleoprotein uncovers distinct features of its nuclear localization. J Virol. 89: 2792-800, 2015. 


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