@article{SchloerHolzloehnerListeketal.2018,
  author    = {Schl{\"o}r, Anja and Holzl{\"o}hner, Pamela and Listek, Martin and Grieß, Cindy and Butze, Monique and Micheel, Burkhard and Hentschel, Christian and Sowa, Mandy and Roggenbuck, Dirk and Schierack, Peter and F{\"u}ner, Jonas and Schliebs, Erik and Goihl, Alexander and Reinhold, Dirk and Hanack, Katja},
  title     = {Generation and validation of murine monoclonal and camelid recombinant single domain antibodies specific for human pancreatic glycoprotein 2},
  series = {New biotechnology},
  volume    = {45},
  journal   = {New biotechnology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1871-6784},
  doi       = {10.1016/j.nbt.2018.03.006},
  pages     = {60 -- 68},
  year      = {2018},
  abstract  = {Pancreatic secretory zymogen-granule membrane glycoprotein 2 (GP2) has been identified as a major autoantigenic target in Crohn's disease patients. It was reported recently that a long (GP2a) and a short (GP2b) isoform of GP2 exist and that in the outcome of inflammatory bowel diseases (IBD) GP2-specific autoantibodies probably appear as new serological markers for diagnosis and therapeutic monitoring. To investigate this further and in order to establish diagnostic tools for the discrimination of both GP2 isoforms, a set of different murine monoclonal and camelid recombinant single domain antibodies (camelid VHH) was generated and validated in various enzyme-linked immunosorbent assay (ELISA) formats, immunofluorescence on transgenic cell lines and immunohistochemistry on monkey pancreas tissue sections. Out of six binders identified, one was validated as highly specific for GP2a. This murine monoclonal antibody (mAb) was used as capture antibody in construction of a sandwich ELISA for the detection of GP2a. Camelid VHHs or a second murine mAb served as detection antibodies in this system. All antibodies were also able to stain GP2a or GP2b on transgenic cell lines as well as on pancreatic tissue in immunohistochemistry. The KD values measured for the camelid VHHs were between 7 nM and 23pM. This set of specific binders will enable the development of suitable diagnostic tools for GP2-related studies in IBD.},
  language  = {en}
}
@article{HolzloehnerButzeMaieretal.2018,
  author    = {Holzl{\"o}hner, Pamela and Butze, Monique and Maier, Natalia and Hebel, Nicole and Schliebs, Erik and Micheel, Burkhard and Fuener, Jonas and Heidicke, Gabriele and Hanack, Katja},
  title     = {Generation of murine monoclonal antibodies with specificity against conventional camelid IgG1 and heavy-chain only IgG2/3},
  series = {Veterinary Immunology and Immunopathology},
  volume    = {197},
  journal   = {Veterinary Immunology and Immunopathology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0165-2427},
  doi       = {10.1016/j.vetimm.2018.01.006},
  pages     = {1 -- 6},
  year      = {2018},
  abstract  = {Camelids possess antibodies with a conventional four-chain structure consisting of two heavy and two light chains (of subclass IgG1) but further they also generate heavy-chain only antibodies (of subclass IgG2 and 3) which are fully functional in antigen binding. In this study subclass-specific murine monoclonal antibodies specific to conventional camelid IgG1 and heavy-chain only IgG2/3 were generated and validated for the use as potent secondary detection reagents. The monoclonal antibodies are able to differentiate between all camelid IgGs, conventional four-chain camelid antibodies (of subclass IgG1) and exclusively heavy chain-only antibodies (of subclasses IgG2 and IgG3). Further these antibodies were used to detect specific immune responses after vaccination of Camelids against bovine corona- and rotavirus strains and different E.coli. and Clostridia - antigens and to identify Erysipelothrix rhusiopathiae infected animals within a herd. The described antibodies are suitable as new secondary agents for the detection of different camelid subclasses and the validation of camelid immune reactions.},
  language  = {en}
}
@misc{HanackSchloerHolzloehneretal.2016,
  author    = {Hanack, Katja and Schloer, Anja and Holzloehner, Pamela and Listek, Martin and Bauer, Cindy and Butze, Monique and Micheel, Burkhard and Hentschel, Christian and Sowa, Mandy and Roggenbuck, Dirk and Schierack, Peter and Fuener, Jonas and Schliebs, Erik and Goihl, Alexander and Reinhold, Dirk},
  title     = {Camelid nanobodies specific to human pancreatic glycoprotein 2},
  series = {The journal of immunology},
  volume    = {196},
  journal   = {The journal of immunology},
  publisher = {American Assoc. of Immunologists},
  address   = {Bethesda},
  issn      = {0022-1767},
  pages     = {313 -- 328},
  year      = {2016},
  abstract  = {Pancreatic secretory zymogen-granule membrane glycoprotein 2 (GP2) has been identified to be a major autoantigenic target in Crohn's disease patients. It was discussed recently that a long and a short isoform of GP2 exists whereas the short isoform is often detected by GP2-specific autoantibodies. In the outcome of inflammatory bowel diseases, these GP2-specific autoantibodies are discussed as new serological markers for diagnosis and therapeutic monitoring. To investigate this further, camelid nanobodies were generated by phage display and selected against the short isoform of GP2 in order to isolate specific tools for the discrimination of both isoforms. Nanobodies are single domain antibodies derived from camelid heavy chain only antibodies and characterized by a high stability and solubility. The selected candidates were expressed, purified and validated regarding their binding properties in different enzyme-linked immunosorbent assays formats, immunofluorescence, immunohistochemistry and surface plasmon resonance spectroscopy. Four different nanobodies could be selected whereof three recognize the short isoform of GP2 very specifically and one nanobody showed a high binding capacity for both isoforms. The KD values measured for all nanobodies were between 1.3 nM and 2.3 pM indicating highly specific binders suitable for the application as diagnostic tool in inflammatory bowel disease.},
  language  = {en}
}
@misc{HolzloehnerButzeHebeletal.2016,
  author    = {Holzl{\"o}hner, Pamela and Butze, Monique and Hebel, Nicole and Weschke, Daniel and Schliebs, E. and Naumann, F. and F{\"u}ner, J. and Micheel, Burkhard and Hanack, Katja},
  title     = {Monoclonal mouse antibodies against PBMC subpopulations of New World camelides},
  series = {European journal of immunology},
  volume    = {46},
  journal   = {European journal of immunology},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0014-2980},
  pages     = {1175 -- 1175},
  year      = {2016},
  language  = {en}
}