The authors unintentionally overlooked a recent publication that provides a detailed analysis of the affinity of the receptors for the Fc region of IgG (FcγRs) for different IgG isotypes, based on data from both surface plasmon resonance and binding to the surface of transfected cells1. The key finding of this paper was to accurately determine the high affinity of IgG3 for FcγRIIIA and FcγRIIIB, which is underestimated by surface plasmon resonance experiments owing to the long hinge region that influences accessibility of IgG3. This finding underpins the strong activating effect of IgG3, particularly on myeloid cells (for example, see Ref. 2). A modified version of Fig. 1 is shown below to reflect these findings. The authors would like to thank G. Vidarsson of the Department of Experimental Immunohematology, Sanquin Research, and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands, for bringing this to their attention.
References
Bruhns, P. et al. Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses. Blood 113, 3716–3725 (2009).
Vidarsson, G. et al. Activity of human IgG and IgA subclasses in immune defense against Neisseria meningitidis serogroup B. J. Immunol. 166, 6250–6256 (2001).
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The online version of the original article can be found at 10.1038/nri2762
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Smith, K., Clatworthy, M. Erratum: FcγRIIB in autoimmunity and infection: evolutionary and therapeutic implications. Nat Rev Immunol 10, 674 (2010). https://doi.org/10.1038/nri2821
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DOI: https://doi.org/10.1038/nri2821