We are delighted to announce that our novel STR silencing technology has been recently published in the peer reviewed and open access journal PLoS ONE. This is available to download by clicking on the image below. We would like to thank all our partners that contributed to this work: Absolute Antibody, ProImmune, Antibody Analytics, Reading Scientific Services Limited, Celentyx and Abzena.
From the abstract:
Elimination of the binding of immunoglobulin Fc to Fc gamma receptors (FcγR) is highly desirable for the avoidance of unwanted inflammatory responses to therapeutic antibodies and fusion proteins. Many different approaches have been described in the literature but none of them completely eliminates binding to all of the Fcγ receptors. Here we describe a set of novel variants having specific amino acid substitutions in the Fc region at L234 and L235 combined with the substitution G236R. They show no detectable binding to Fcγ receptors or to C1q, are inactive in functional cell-based assays and do not elicit inflammatory cytokine responses. Meanwhile, binding to FcRn, manufacturability, stability and potential for immunogenicity are unaffected. These variants have the potential to improve the safety and efficacy of therapeutic antibodies and Fc fusion proteins.