Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?

Siqi Gong; Seijal Gautam; Joshua D Coneglio; Hanna B Scinto; Ruth M Ruprecht

doi:10.3390/antib11020037

Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?

Antibodies (Basel). 2022 May 18;11(2):37. doi: 10.3390/antib11020037.

Authors

Siqi Gong^{1

2

3}, Seijal Gautam^{1

4}, Joshua D Coneglio¹, Hanna B Scinto^{2

3}, Ruth M Ruprecht^{1

2

3

4}

Affiliations

¹ New Iberia Research Center, University of Louisiana at Lafayette, New Iberia, LA 70560, USA.
² Department of Microbiology, Immunology & Molecular Genetics, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
³ Department of Virology and Immunology, Texas Biomedical Research Institute, San Antonio, TX 78227, USA.
⁴ Department of Biology, University of Louisiana at Lafayette, Lafayette, LA 70503, USA.

Abstract

When constructing isogenic recombinant IgM-IgG pairs, we discovered that μ heavy chains strongly prefer partnering with λ light chains for optimal IgM expression in transiently cotransfected Expi293 cells. When μ chains were paired with κ light chains, IgM yields were low but increased by logs-up to 20,000 X-by using λ chains instead. Switching light chains did not alter epitope specificity. For dimeric IgA2, optimal expression involved pairing with λ chains, whereas light-chain preference varied for other immunoglobulin classes. In summary, recombinant IgM production can be drastically increased by using λ chains, an important finding in the use of IgM for mucosal immunoprophylaxis.

Keywords: lambda light-chain preference; mAb yield; monoclonal antibody; recombinant IgG; recombinant IgM; recombinant dIgA.

Abstract

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