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  • 1.
    Volk, Anna-Luisa
    et al.
    KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology. School of Biotechnology (BIO), KTH, Centres, Science for Life Laboratory, SciLifeLab, KTH Center for Applied Proteomics (KCAP).
    Hu, Francis Jingxin
    KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology. School of Biotechnology (BIO), KTH, Centres, Science for Life Laboratory, SciLifeLab, KTH Center for Applied Proteomics (KCAP).
    Berglund, Magnus M.
    Nordling, Erik
    Strömberg, Patrik
    Uhlén, Mathias
    KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology. KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH - Center for Applied Proteomics; Technical University of Denmark, Denmark.
    Rockberg, Johan
    KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology. KTH - Center for Applied Proteomics.
    Stratification of responders towards eculizumab using a structural epitope mapping strategy2016In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, article id 31365Article in journal (Refereed)
    Abstract [en]

    The complement component 5 (C5)-binding antibody eculizumab is used to treat patients with paroxysmal nocturnal hemoglobinuria (PNH) and atypical haemolytic uremic syndrome (aHUS). As recently reported there is a need for a precise classification of eculizumab responsive patients to allow for a safe and cost-effective treatment. To allow for such stratification, knowledge of the precise binding site of the drug on its target is crucial. Using a structural epitope mapping strategy based on bacterial surface display, flow cytometric sorting and validation via haemolytic activity testing, we identified six residues essential for binding of eculizumab to C5. This epitope co-localizes with the contact area recently identified by crystallography and includes positions in C5 mutated in non-responders. The identified epitope also includes residue W917, which is unique for human C5 and explains the observed lack of cross-reactivity for eculizumab with other primates. We could demonstrate that Ornithodorus moubata complement inhibitor (OmCI), in contrast to eculizumab, maintained anti-haemolytic function for mutations in any of the six epitope residues, thus representing a possible alternative treatment for patients non-responsive to eculizumab. The method for stratification of patients described here allows for precision medicine and should be applicable to several other diseases and therapeutics.

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