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Highly active engineered IgG3 antibodies against SARS-CoV-2.
Kallolimath, Somanath; Sun, Lin; Palt, Roman; Stiasny, Karin; Mayrhofer, Patrick; Gruber, Clemens; Kogelmann, Benjamin; Chen, Qiang; Steinkellner, Herta.
  • Kallolimath S; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1180 Vienna, Austria.
  • Sun L; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1180 Vienna, Austria.
  • Palt R; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1180 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, 1180 Vienna, Austria.
  • Gruber C; Core Facility Mass Spectrometry, University of Natural Resources and Life Sciences, 1180 Vienna, Austria.
  • Kogelmann B; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1180 Vienna, Austria.
  • Chen Q; The Biodesign Institute and School of Life Sciences, Arizona State University, Tempe, AZ 85281.
  • Steinkellner H; Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1180 Vienna, Austria; herta.steinkellner@boku.ac.at.
Proc Natl Acad Sci U S A ; 118(42)2021 10 01.
Artigo em Inglês | MEDLINE | ID: covidwho-1447423
ABSTRACT
Monoclonal antibodies (mAbs) that efficiently neutralize SARS-CoV-2 have been developed at an unprecedented speed. Notwithstanding, there is a vague understanding of the various Ab functions induced beyond antigen binding by the heavy-chain constant domain. To explore the diverse roles of Abs in SARS-CoV-2 immunity, we expressed a SARS-CoV-2 spike protein (SP) binding mAb (H4) in the four IgG subclasses present in human serum (IgG1-4) using glyco-engineered Nicotiana benthamiana plants. All four subclasses, carrying the identical antigen-binding site, were fully assembled in planta and exhibited a largely homogeneous xylose- and fucose-free glycosylation profile. The Ab variants ligated to the SP with an up to fivefold increased binding activity of IgG3. Furthermore, all H4 subtypes were able to neutralize SARS-CoV-2. However, H4-IgG3 exhibited an up to 50-fold superior neutralization potency compared with the other subclasses. Our data point to a strong protective effect of IgG3 Abs in SARS-CoV-2 infection and suggest that superior neutralization might be a consequence of cross-linking the SP on the viral surface. This should be considered in therapy and vaccine development. In addition, we underscore the versatile use of plants for the rapid expression of complex proteins in emergency cases.
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Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: MEDLINE Assunto principal: Imunoglobulina G / Glicoproteína da Espícula de Coronavírus / SARS-CoV-2 / COVID-19 / Anticorpos Monoclonais / Anticorpos Antivirais Tipo de estudo: Estudo observacional / Ensaios controlados aleatorizados Tópicos: Vacinas / Variantes Limite: Humanos Idioma: Inglês Ano de publicação: 2021 Tipo de documento: Artigo País de afiliação: Pnas.2107249118

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Texto completo: Disponível Coleções: Bases de dados internacionais Base de dados: MEDLINE Assunto principal: Imunoglobulina G / Glicoproteína da Espícula de Coronavírus / SARS-CoV-2 / COVID-19 / Anticorpos Monoclonais / Anticorpos Antivirais Tipo de estudo: Estudo observacional / Ensaios controlados aleatorizados Tópicos: Vacinas / Variantes Limite: Humanos Idioma: Inglês Ano de publicação: 2021 Tipo de documento: Artigo País de afiliação: Pnas.2107249118