Isolation and characterization of a monoclonal antibody containing an extra heavy-light chain Fab arm
Autor: | Darren Brown, Dan Boyd, Alexandre Ambrogelly, Jenny Wang, Arpa Ebrahimi, Brian Mickus, Matthew R. Schenauer, Sarah Ronan |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
medicine.drug_class Immunology Size-exclusion chromatography Immunoglobulin light chain Monoclonal antibody Antibodies Monoclonal Humanized 030226 pharmacology & pharmacy Genome 03 medical and health sciences chemistry.chemical_compound Immunoglobulin Fab Fragments 0302 clinical medicine medicine Immunology and Allergy Humans Chemistry Brief Report Fc domain 030104 developmental biology Monomer Biochemistry Cell culture Immunoglobulin G Immunoglobulin Heavy Chains Function (biology) |
Zdroj: | mAbs. 10(3) |
ISSN: | 1942-0870 |
Popis: | Isolation and characterization of monoclonal antibody (mAb) variants to understand the impact of their structure on function is a typical activity during early-stage candidate selection that contributes to derisking clinical development. In particular, efforts are devoted to characterizing oligomeric variants, owing to their potential immunogenic nature. We report here a mAb variant consisting of a canonical mAb monomer associated in a non-covalent fashion with an antigen-binding fragment (Fab) arm amputated from its Fc domain. The truncated heavy chain is encoded in the cell line genome and is the likely product of a genomic recombination during cell line generation. The addition of the Fab arm results in severe loss of potency, indicating its interaction with the Fab domain of the monomer. The presence of such a variant can easily be mitigated by an adequate purification step. |
Databáze: | OpenAIRE |
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