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Seed-produced anti-globulin VHH-Fc antibodies retrieve globulin precursors in the insoluble fraction and modulate the Arabidopsis thaliana seed subcellular morphology

Thomas De Meyer, Elsa Arcalis, Stanislav Melnik, Katrien Maleux (UGent) , Jonah Nolf (UGent) , Friedrich Altmann, Anna Depicker (UGent) and Eva Stöger
(2020) PLANT MOLECULAR BIOLOGY. 103. p.597-608
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Abstract
Key message Nanobody-heavy chain (VHH-Fc) antibody formats have the potential to immunomodulate even highly accumulating proteins and provide a valuable tool to experimentally modulate the subcellular distribution of seed storage proteins. Recombinant antibodies often obtain high accumulation levels in plants, and thus, besides being the actual end-product, antibodies targeting endogenous host proteins can be used to interfere with the localization and functioning of their corresponding antigens. Here, we compared the effect of a seed-expressed nanobody-heavy chain (VHH-Fc) antibody against the highly abundant Arabidopsis thaliana globulin seed storage protein cruciferin with that of a VHH-Fc antibody without endogenous target. Both antibodies reached high accumulation levels of around 10% of total soluble protein, but strikingly, another significant part was present in the insoluble protein fraction and was recovered only after extraction under denaturing conditions. In seeds containing the anti-cruciferin antibodies but not the antibody without endogenous target, the amount of soluble, processed globulin subunits was severely reduced and a major part of the cruciferin molecules was found as precursor in the insoluble fraction. Moreover, in these seeds, aberrant vacuolar phenotypes were observed that were different from the effects caused by the depletion of globulins in knock-out seeds. Remarkably, the seeds with strongly reduced globulin amounts are fully viable and germinate with frequencies similar to wild type, illustrating how flexible seeds can retrieve amino acids from the stored proteins to start germination.
Keywords
Protein storage vacuole, Seed storage protein, Russell-like bodies, VHH-Fc fusions, Immunomodulation, Molecular farming, FUSARIUM-SPECIFIC ANTIBODY, CHAIN FV-ANTIBODY, NICOTIANA-BENTHAMIANA, ENHANCES TOLERANCE, STORAGE PROTEINS, TOBACCO PLANTS, IN-VITRO, EXPRESSION, IMMUNOMODULATION, VIRUS

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MLA
De Meyer, Thomas, et al. “Seed-Produced Anti-Globulin VHH-Fc Antibodies Retrieve Globulin Precursors in the Insoluble Fraction and Modulate the Arabidopsis Thaliana Seed Subcellular Morphology.” PLANT MOLECULAR BIOLOGY, vol. 103, 2020, pp. 597–608, doi:10.1007/s11103-020-01007-w.
APA
De Meyer, T., Arcalis, E., Melnik, S., Maleux, K., Nolf, J., Altmann, F., … Stöger, E. (2020). Seed-produced anti-globulin VHH-Fc antibodies retrieve globulin precursors in the insoluble fraction and modulate the Arabidopsis thaliana seed subcellular morphology. PLANT MOLECULAR BIOLOGY, 103, 597–608. https://doi.org/10.1007/s11103-020-01007-w
Chicago author-date
De Meyer, Thomas, Elsa Arcalis, Stanislav Melnik, Katrien Maleux, Jonah Nolf, Friedrich Altmann, Anna Depicker, and Eva Stöger. 2020. “Seed-Produced Anti-Globulin VHH-Fc Antibodies Retrieve Globulin Precursors in the Insoluble Fraction and Modulate the Arabidopsis Thaliana Seed Subcellular Morphology.” PLANT MOLECULAR BIOLOGY 103: 597–608. https://doi.org/10.1007/s11103-020-01007-w.
Chicago author-date (all authors)
De Meyer, Thomas, Elsa Arcalis, Stanislav Melnik, Katrien Maleux, Jonah Nolf, Friedrich Altmann, Anna Depicker, and Eva Stöger. 2020. “Seed-Produced Anti-Globulin VHH-Fc Antibodies Retrieve Globulin Precursors in the Insoluble Fraction and Modulate the Arabidopsis Thaliana Seed Subcellular Morphology.” PLANT MOLECULAR BIOLOGY 103: 597–608. doi:10.1007/s11103-020-01007-w.
Vancouver
1.
De Meyer T, Arcalis E, Melnik S, Maleux K, Nolf J, Altmann F, et al. Seed-produced anti-globulin VHH-Fc antibodies retrieve globulin precursors in the insoluble fraction and modulate the Arabidopsis thaliana seed subcellular morphology. PLANT MOLECULAR BIOLOGY. 2020;103:597–608.
IEEE
[1]
T. De Meyer et al., “Seed-produced anti-globulin VHH-Fc antibodies retrieve globulin precursors in the insoluble fraction and modulate the Arabidopsis thaliana seed subcellular morphology,” PLANT MOLECULAR BIOLOGY, vol. 103, pp. 597–608, 2020.
@article{8660374,
  abstract     = {{Key message Nanobody-heavy chain (VHH-Fc) antibody formats have the potential to immunomodulate even highly accumulating proteins and provide a valuable tool to experimentally modulate the subcellular distribution of seed storage proteins. Recombinant antibodies often obtain high accumulation levels in plants, and thus, besides being the actual end-product, antibodies targeting endogenous host proteins can be used to interfere with the localization and functioning of their corresponding antigens. Here, we compared the effect of a seed-expressed nanobody-heavy chain (VHH-Fc) antibody against the highly abundant Arabidopsis thaliana globulin seed storage protein cruciferin with that of a VHH-Fc antibody without endogenous target. Both antibodies reached high accumulation levels of around 10% of total soluble protein, but strikingly, another significant part was present in the insoluble protein fraction and was recovered only after extraction under denaturing conditions. In seeds containing the anti-cruciferin antibodies but not the antibody without endogenous target, the amount of soluble, processed globulin subunits was severely reduced and a major part of the cruciferin molecules was found as precursor in the insoluble fraction. Moreover, in these seeds, aberrant vacuolar phenotypes were observed that were different from the effects caused by the depletion of globulins in knock-out seeds. Remarkably, the seeds with strongly reduced globulin amounts are fully viable and germinate with frequencies similar to wild type, illustrating how flexible seeds can retrieve amino acids from the stored proteins to start germination.}},
  author       = {{De Meyer, Thomas and Arcalis, Elsa and Melnik, Stanislav and Maleux, Katrien and Nolf, Jonah and Altmann, Friedrich and Depicker, Anna and Stöger, Eva}},
  issn         = {{0167-4412}},
  journal      = {{PLANT MOLECULAR BIOLOGY}},
  keywords     = {{Protein storage vacuole,Seed storage protein,Russell-like bodies,VHH-Fc fusions,Immunomodulation,Molecular farming,FUSARIUM-SPECIFIC ANTIBODY,CHAIN FV-ANTIBODY,NICOTIANA-BENTHAMIANA,ENHANCES TOLERANCE,STORAGE PROTEINS,TOBACCO PLANTS,IN-VITRO,EXPRESSION,IMMUNOMODULATION,VIRUS}},
  language     = {{eng}},
  pages        = {{597--608}},
  title        = {{Seed-produced anti-globulin VHH-Fc antibodies retrieve globulin precursors in the insoluble fraction and modulate the Arabidopsis thaliana seed subcellular morphology}},
  url          = {{http://doi.org/10.1007/s11103-020-01007-w}},
  volume       = {{103}},
  year         = {{2020}},
}
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