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

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...

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Autores principales: Gong, Siqi, Gautam, Seijal, Coneglio, Joshua D., Scinto, Hanna B., Ruprecht, Ruth M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9149950/
https://www.ncbi.nlm.nih.gov/pubmed/35645210
http://dx.doi.org/10.3390/antib11020037
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author Gong, Siqi
Gautam, Seijal
Coneglio, Joshua D.
Scinto, Hanna B.
Ruprecht, Ruth M.
author_facet Gong, Siqi
Gautam, Seijal
Coneglio, Joshua D.
Scinto, Hanna B.
Ruprecht, Ruth M.
author_sort Gong, Siqi
collection PubMed
description 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.
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spelling pubmed-91499502022-05-31 Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells? Gong, Siqi Gautam, Seijal Coneglio, Joshua D. Scinto, Hanna B. Ruprecht, Ruth M. Antibodies (Basel) Communication 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. MDPI 2022-05-18 /pmc/articles/PMC9149950/ /pubmed/35645210 http://dx.doi.org/10.3390/antib11020037 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Gong, Siqi
Gautam, Seijal
Coneglio, Joshua D.
Scinto, Hanna B.
Ruprecht, Ruth M.
Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?
title Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?
title_full Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?
title_fullStr Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?
title_full_unstemmed Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?
title_short Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?
title_sort antibody light chains: key to increased monoclonal antibody yields in expi293 cells?
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9149950/
https://www.ncbi.nlm.nih.gov/pubmed/35645210
http://dx.doi.org/10.3390/antib11020037
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