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Increased in vitro neutralizing activity of SARS-CoV-2 IgA1 dimers compared to monomers and IgG.
Sun, Lin; Kallolimath, Somanath; Palt, Roman; Stiasny, Karin; Mayrhofer, Patrick; Maresch, Daniel; Eidenberger, Lukas; Steinkellner, Herta.
  • Sun L; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Kallolimath S; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Palt R; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Stiasny K; Center for Virology, Medical University of Vienna, 1090 Vienna, Austria.
  • Mayrhofer P; Department of Biotechnology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Maresch D; Core Facility Mass Spectrometry, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Eidenberger L; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
  • Steinkellner H; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria; herta.steinkellner@boku.ac.at.
Proc Natl Acad Sci U S A ; 118(44)2021 11 02.
Article in English | MEDLINE | ID: covidwho-1493344
ABSTRACT
Here, we expressed two neutralizing monoclonal antibodies (Abs) against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2; H4 and B38) in three formats IgG1, IgA1 monomers (m), and IgA1 dimers (d) in glycoengineered Nicotiana benthamiana plants. All six Ab variants assembled properly and exhibited a largely homogeneous glycosylation profile. Despite modest variation in antigen binding between Ab formats, SARS-CoV-2 neutralization (NT) potency significantly increased in the following manner IgG1 < IgA1-m < IgA1-d, with an up to 240-fold NT increase of dimers compared to corresponding monomers. Our results underscore that both IgA's structural features and multivalency positively impact NT potency. In addition, they emphasize the versatile use of plants for the rapid expression of complex human proteins.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Immunoglobulin A / Immunoglobulin G / SARS-CoV-2 / COVID-19 / Antibodies, Monoclonal Limits: Animals / Humans Language: English Year: 2021 Document Type: Article Affiliation country: Pnas.2107148118

Full text: Available Collection: International databases Database: MEDLINE Main subject: Immunoglobulin A / Immunoglobulin G / SARS-CoV-2 / COVID-19 / Antibodies, Monoclonal Limits: Animals / Humans Language: English Year: 2021 Document Type: Article Affiliation country: Pnas.2107148118