Fc Binding by Fc gamma RIIa Is Essential for Cellular Activation by the Anti-Fc gamma RIIa mAbs 8.26 and 8.2
Bruce D Wines, Halina M Trist, Sandra Esparon, Rachael E Impey, Graham A Mackay, Robert K Andrews, Tatiana P Soares da Costa, Geoffrey A Pietersz, Ross Baker, P Mark Hogarth
FRONTIERS IN IMMUNOLOGY | FRONTIERS MEDIA SA | Published : 2021
FcγR activity underpins the role of antibodies in both protective immunity and auto-immunity and importantly, the therapeutic activity of many monoclonal antibody therapies. Some monoclonal anti-FcγR antibodies activate their receptors, but the properties required for cell activation are not well defined. Here we examined activation of the most widely expressed human FcγR; FcγRIIa, by two non-blocking, mAbs, 8.26 and 8.2. Crosslinking of FcγRIIa by the mAb F(ab')2 regions alone was insufficient for activation, indicating activation also required receptor engagement by the Fc region. Similarly, when mutant receptors were inactivated in the Fc binding site, so that intact mAb was only able to ..View full abstract
Awarded by Australian NHRMC - Project Grant
Awarded by Australian Research Council fellowship
This work was supported by the Australian NHRMC -Project Grant, to PH and BW (GNT1145303). Support to the Burnet Institute comes from the NHMRC Independent Research Institutes Infrastructure Support Scheme and a Victorian State Government Operational Infrastructure grant. TC holds an Australian Research Council fellowship (DE190100806).