An oligosaccharyltransferase from Leishmania donovani increases the N-glycan occupancy on plant-produced IgG1
N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of...
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| Published in | Frontiers in plant science Vol. 14; p. 1233666 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Frontiers Media S.A
08.08.2023
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1664-462X 1664-462X |
| DOI | 10.3389/fpls.2023.1233666 |
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| Abstract | N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of unglycosylated Fc domain. To overcome this limitation, we tested a single-subunit oligosaccharyltransferase from the protozoan
Leishmania donovani
(LdOST) for its ability to improve IgG1 Fc glycosylation. LdOST fused to a fluorescent protein was transiently expressed in
Nicotiana benthamiana
and confocal microscopy confirmed the subcellular location at the endoplasmic reticulum. Transient co-expression of LdOST with two different IgG1 antibodies resulted in a significant increase (up to 97%) of Fc glycosylation while leaving the overall N-glycan composition unmodified, as determined by different mass spectrometry approaches. While biochemical and functional features of “glycosylation improved” antibodies remained unchanged, a slight increase in FcγRIIIa binding and thermal stability was observed. Collectively, our results reveal that LdOST expression is suitable to reduce the heterogeneity of plant-produced antibodies and can contribute to improving their stability and effector functions. |
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| AbstractList | N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of unglycosylated Fc domain. To overcome this limitation, we tested a single-subunit oligosaccharyltransferase from the protozoan
(LdOST) for its ability to improve IgG1 Fc glycosylation. LdOST fused to a fluorescent protein was transiently expressed in
and confocal microscopy confirmed the subcellular location at the endoplasmic reticulum. Transient co-expression of LdOST with two different IgG1 antibodies resulted in a significant increase (up to 97%) of Fc glycosylation while leaving the overall N-glycan composition unmodified, as determined by different mass spectrometry approaches. While biochemical and functional features of "glycosylation improved" antibodies remained unchanged, a slight increase in FcγRIIIa binding and thermal stability was observed. Collectively, our results reveal that LdOST expression is suitable to reduce the heterogeneity of plant-produced antibodies and can contribute to improving their stability and effector functions. N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of unglycosylated Fc domain. To overcome this limitation, we tested a single-subunit oligosaccharyltransferase from the protozoan Leishmania donovani (LdOST) for its ability to improve IgG1 Fc glycosylation. LdOST fused to a fluorescent protein was transiently expressed in Nicotiana benthamiana and confocal microscopy confirmed the subcellular location at the endoplasmic reticulum. Transient co-expression of LdOST with two different IgG1 antibodies resulted in a significant increase (up to 97%) of Fc glycosylation while leaving the overall N-glycan composition unmodified, as determined by different mass spectrometry approaches. While biochemical and functional features of “glycosylation improved” antibodies remained unchanged, a slight increase in FcγRIIIa binding and thermal stability was observed. Collectively, our results reveal that LdOST expression is suitable to reduce the heterogeneity of plant-produced antibodies and can contribute to improving their stability and effector functions. N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of unglycosylated Fc domain. To overcome this limitation, we tested a single-subunit oligosaccharyltransferase from the protozoan Leishmania donovani (LdOST) for its ability to improve IgG1 Fc glycosylation. LdOST fused to a fluorescent protein was transiently expressed in Nicotiana benthamiana and confocal microscopy confirmed the subcellular location at the endoplasmic reticulum. Transient co-expression of LdOST with two different IgG1 antibodies resulted in a significant increase (up to 97%) of Fc glycosylation while leaving the overall N-glycan composition unmodified, as determined by different mass spectrometry approaches. While biochemical and functional features of “glycosylation improved” antibodies remained unchanged, a slight increase in FcγRIIIa binding and thermal stability was observed. Collectively, our results reveal that LdOST expression is suitable to reduce the heterogeneity of plant-produced antibodies and can contribute to improving their stability and effector functions. N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of unglycosylated Fc domain. To overcome this limitation, we tested a single-subunit oligosaccharyltransferase from the protozoan Leishmania donovani (LdOST) for its ability to improve IgG1 Fc glycosylation. LdOST fused to a fluorescent protein was transiently expressed in Nicotiana benthamiana and confocal microscopy confirmed the subcellular location at the endoplasmic reticulum. Transient co-expression of LdOST with two different IgG1 antibodies resulted in a significant increase (up to 97%) of Fc glycosylation while leaving the overall N-glycan composition unmodified, as determined by different mass spectrometry approaches. While biochemical and functional features of "glycosylation improved" antibodies remained unchanged, a slight increase in FcγRIIIa binding and thermal stability was observed. Collectively, our results reveal that LdOST expression is suitable to reduce the heterogeneity of plant-produced antibodies and can contribute to improving their stability and effector functions.N-Glycosylation of immunoglobulin G1 (IgG1) at the heavy chain Fc domain (Asn297) plays an important role for antibody structure and effector functions. While numerous recombinant IgG1 antibodies have been successfully expressed in plants, they frequently display a considerable amount (up to 50%) of unglycosylated Fc domain. To overcome this limitation, we tested a single-subunit oligosaccharyltransferase from the protozoan Leishmania donovani (LdOST) for its ability to improve IgG1 Fc glycosylation. LdOST fused to a fluorescent protein was transiently expressed in Nicotiana benthamiana and confocal microscopy confirmed the subcellular location at the endoplasmic reticulum. Transient co-expression of LdOST with two different IgG1 antibodies resulted in a significant increase (up to 97%) of Fc glycosylation while leaving the overall N-glycan composition unmodified, as determined by different mass spectrometry approaches. While biochemical and functional features of "glycosylation improved" antibodies remained unchanged, a slight increase in FcγRIIIa binding and thermal stability was observed. Collectively, our results reveal that LdOST expression is suitable to reduce the heterogeneity of plant-produced antibodies and can contribute to improving their stability and effector functions. |
| Author | Ruocco, Valentina Lavoie, Pierre-Olivier Gach, Johannes S. Steinkellner, Herta König-Beihammer, Julia Kogelmann, Benjamin Beihammer, Gernot Grünwald-Gruber, Clemens D’Aoust, Marc-André Strasser, Richard Saxena, Pooja |
| AuthorAffiliation | 4 Medicago Inc. , Quebec, QC , Canada 1 Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences , Vienna , Austria 5 Division of Infectious Diseases, University of California, Irvine , Irvine, CA , United States 3 Core Facility Mass Spectrometry, University of Natural Resources and Life Sciences , Vienna , Austria 2 acib - Austrian Centre of Industrial Biotechnology , Vienna , Austria |
| AuthorAffiliation_xml | – name: 5 Division of Infectious Diseases, University of California, Irvine , Irvine, CA , United States – name: 2 acib - Austrian Centre of Industrial Biotechnology , Vienna , Austria – name: 3 Core Facility Mass Spectrometry, University of Natural Resources and Life Sciences , Vienna , Austria – name: 1 Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences , Vienna , Austria – name: 4 Medicago Inc. , Quebec, QC , Canada |
| Author_xml | – sequence: 1 givenname: Gernot surname: Beihammer fullname: Beihammer, Gernot – sequence: 2 givenname: Julia surname: König-Beihammer fullname: König-Beihammer, Julia – sequence: 3 givenname: Benjamin surname: Kogelmann fullname: Kogelmann, Benjamin – sequence: 4 givenname: Valentina surname: Ruocco fullname: Ruocco, Valentina – sequence: 5 givenname: Clemens surname: Grünwald-Gruber fullname: Grünwald-Gruber, Clemens – sequence: 6 givenname: Marc-André surname: D’Aoust fullname: D’Aoust, Marc-André – sequence: 7 givenname: Pierre-Olivier surname: Lavoie fullname: Lavoie, Pierre-Olivier – sequence: 8 givenname: Pooja surname: Saxena fullname: Saxena, Pooja – sequence: 9 givenname: Johannes S. surname: Gach fullname: Gach, Johannes S. – sequence: 10 givenname: Herta surname: Steinkellner fullname: Steinkellner, Herta – sequence: 11 givenname: Richard surname: Strasser fullname: Strasser, Richard |
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| CitedBy_id | crossref_primary_10_1016_j_copbio_2024_103145 crossref_primary_10_3390_antib13020029 crossref_primary_10_3389_fpls_2024_1531710 crossref_primary_10_3389_fbioe_2023_1320586 |
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| ContentType | Journal Article |
| Copyright | Copyright © 2023 Beihammer, König-Beihammer, Kogelmann, Ruocco, Grünwald-Gruber, D’Aoust, Lavoie, Saxena, Gach, Steinkellner and Strasser. Copyright © 2023 Beihammer, König-Beihammer, Kogelmann, Ruocco, Grünwald-Gruber, D’Aoust, Lavoie, Saxena, Gach, Steinkellner and Strasser 2023 Beihammer, König-Beihammer, Kogelmann, Ruocco, Grünwald-Gruber, D’Aoust, Lavoie, Saxena, Gach, Steinkellner and Strasser |
| Copyright_xml | – notice: Copyright © 2023 Beihammer, König-Beihammer, Kogelmann, Ruocco, Grünwald-Gruber, D’Aoust, Lavoie, Saxena, Gach, Steinkellner and Strasser. – notice: Copyright © 2023 Beihammer, König-Beihammer, Kogelmann, Ruocco, Grünwald-Gruber, D’Aoust, Lavoie, Saxena, Gach, Steinkellner and Strasser 2023 Beihammer, König-Beihammer, Kogelmann, Ruocco, Grünwald-Gruber, D’Aoust, Lavoie, Saxena, Gach, Steinkellner and Strasser |
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| Keywords | glycosylation Nicotiana benthamiana glycoprotein antibody recombinant protein |
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| Title | An oligosaccharyltransferase from Leishmania donovani increases the N-glycan occupancy on plant-produced IgG1 |
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