Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector Functions

@inproceedings{Monnet2015SelectionOI,
  title={Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector Functions},
  author={C{\'e}line Monnet and Sylvie Jorieux and R{\'e}mi Urbain and Nathalie Fournier and Khalil Bouayadi and Christophe de Romeuf and Christian K. Behrens and Alexandre Fontayne and Philippe Mondon},
  booktitle={Front. Immunol.},
  year={2015}
}
Despite the reasonably long half-life of immunoglogulin G (IgGs), market pressure for higher patient convenience while conserving efficacy continues to drive IgG half-life improvement. IgG half-life is dependent on the neonatal Fc receptor (FcRn), which among other functions, protects IgG from catabolism. FcRn binds the Fc domain of IgG at an acidic pH ensuring that endocytosed IgG will not be degraded in lysosomal compartments and will then be released into the bloodstream. Consistent with… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-10 of 90 references

novel expression vectors that display cloned antigens on the virion surface

  • Smith GP. Filamentous fusion phage
  • Science
  • 1985
Highly Influential
6 Excerpts

biological consequences

  • WF Dall’acqua, RM Woods, +4 authors receptor et al. Increasing the affinity of a human IgG1 for Fc
  • J Immunol
  • 2002
Highly Influential
6 Excerpts

Similar Papers

Loading similar papers…