Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization

Sun L, Palt R, Schütz G, Föderl-Höbenreich E, Brod L, Hermle A, Lux A, Steinkellner H, Kallolimath S (2025)

Publication Type: Journal article

Publication year: 2025

Journal

Antibodies MDPI

Book Volume: 14

Article Number: 50

Journal Issue: 2

DOI: 10.3390/antib14020050

Abstract

Therapeutic antibodies with lambda light chains (λ-Abs) are underrepresented compared to kappa light chains (κ-Abs). Here, we evaluated two SARS-CoV-2-specific monoclonal antibodies (mAbs) that exhibit high (P5C3) and low (H4) antigen binding as κ and λ variants. mAbs expressed in glycoengineered Nicotiana benthamiana did not show differences in expression levels, glycosylation, and antigen binding, while κ-Abs exhibited slightly increased thermodynamic stability over λ-Abs. SARS-CoV-2 neutralization and IgG-FcγR immune complex studies revealed increased activities of H4 IgG1κ compared to H4 IgG1λ, with no differences observed between P5C3 variants. Our results indicate that constant light chain variability and Ab specificity contribute to Ab features, a fact that should be considered in engineering therapeutics.

Authors with CRIS profile

Antonia Hermle Lehrstuhl für Genetik Anja Lux Lehrstuhl für Genetik

Involved external institutions

Universität für Bodenkultur Wien (BOKU) / University of Natural Resources and Life Sciences, Vienna

Austria (AT) Medizinische Universität Graz

Austria (AT)

How to cite

APA:

Sun, L., Palt, R., Schütz, G., Föderl-Höbenreich, E., Brod, L., Hermle, A.,... Kallolimath, S. (2025). Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization. Antibodies, 14(2). https://doi.org/10.3390/antib14020050

MLA:

Sun, Lin, et al. "Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization." Antibodies 14.2 (2025).

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