Functional humanization of immunoglobulin heavy constant gamma 1 Fc domain human
Document Type
Article
Publication Date
2020
Keywords
JMG
JAX Source
Mabs 2020; 12(1):1829334
Volume
12
Issue
1
First Page
1829334
Last Page
1829334
ISSN
1942-0870
PMID
33025844
DOI
https://doi.org/10.1080/19420862.2020.1829334
Grant
OD011190
Abstract
A major asset of many monoclonal antibody (mAb)-based biologics is their persistence in circulation. The MHC class I family Fc receptor, FCGRT, is primarily responsible for this extended pharmacokinetic behavior. Engagement of FCGRT with the crystallizable fragment (Fc) domain protects IgG from catabolic elimination, thereby extending the persistence and bioavailability of IgG and related Fc-based biologics. There is a need for reliable in vivo models to facilitate the preclinical development of novel IgG-based biologics. FcRn-humanized mice have been widely accepted as translationally relevant surrogates for IgG-based biologics evaluations. Although such FCGRT-humanized mice, especially the mouse strain, B6.Cg-Fcgrt
Recommended Citation
Low BE,
Christianson GJ,
Lowell E,
Qin W,
Wiles MV.
Functional humanization of immunoglobulin heavy constant gamma 1 Fc domain human Mabs 2020; 12(1):1829334
Comments
The authors would like to thank Cindy Avery and John Wilson for their excellent technical assistance in this work. Also, Pete Kutny and the microinjection core for their expertise and dedication as well as Simon Lesbirel and the Genome Technology core at The Jackson Laboratory. We also gratefully acknowledge the contribution of Melissa Berry, Derry Roopenian for suggested experimental design and writing and also the Genome Technologies Service and Genetic Engineering Technologies at The Jackson Laboratory for expert assistance with the work described in this publication.