Binding affinities of human IgG1 and chimerized pig and rabbit derivatives to human, pig and rabbit Fc gamma receptor IIIA.

Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE

Original Publication: San Francisco, CA : Public Library of Science

Recombinant Fusion Proteins*; Antibody Affinity/*immunology ; Immunoglobulin G/*immunology ; Immunoglobulin G/*metabolism ; Receptors, IgG/*metabolism; Animals ; Enzyme-Linked Immunosorbent Assay ; Gene Expression ; Humans ; Immunoglobulin G/isolation & purification ; Protein Binding ; Rabbits ; Receptors, IgG/genetics ; Receptors, IgG/isolation & purification ; Surface Plasmon Resonance ; Swine

While pigs and rabbits are used as models for human immune diseases, FcγR binding is poorly characterized in both test species. To evaluate antibody binding to FcγRIIIA, a receptor involved in antibody-dependent cellular cytotoxicity, chimerized antibodies were generated by grafting the variable regions of a human IgG1 onto scaffolds from both species. The affinities of the parent and chimeric antibodies to the FcγRIIIA proteins from all three species were determined. While the human IgG1 and rabbit IgG had similar affinities for each FcγRIIIA with notable differences across species, pig IgG1 only bound pig FcγRIIIA with appreciable affinity. Also, the functional pig and rabbit proteins described here can be used in future experiments, such as pharmacology and mechanism of action studies.
Competing Interests: The authors MMB, AGC and JWT were paid employees at Iconic Therapeutics. This does not alter the authors' adherence to PLOS ONE policies on sharing data and materials.

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0 (Immunoglobulin G)
0 (Receptors, IgG)
0 (Recombinant Fusion Proteins)

Date Created: 20190720 Date Completed: 20200302 Latest Revision: 20200309

20221213

PMC6641210

10.1371/journal.pone.0219999

31323052