Improved Virus Neutralization by Plant-produced Anti-HIV Antibodies with a Homogeneous β1,4-Galactosylated N-Glycan Profile
It is well established that proper N-glycosylation significantly influences the efficacy of monoclonal antibodies (mAbs). However, the specific immunological relevance of individual mAb-associated N-glycan structures is currently largely unknown, because of the heterogeneous N-glycan profiles of mAb...
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| Published in | The Journal of biological chemistry Vol. 284; no. 31; pp. 20479 - 20485 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
9650 Rockville Pike, Bethesda, MD 20814, U.S.A
Elsevier Inc
31.07.2009
American Society for Biochemistry and Molecular Biology |
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| Abstract | It is well established that proper N-glycosylation significantly influences the efficacy of monoclonal antibodies (mAbs). However, the specific immunological relevance of individual mAb-associated N-glycan structures is currently largely unknown, because of the heterogeneous N-glycan profiles of mAbs when produced in mammalian cells. Here we report on the generation of a plant-based expression platform allowing the efficient production of mAbs with a homogeneous β1,4-galactosylated N-glycosylation structure, the major N-glycan species present on serum IgG. This was achieved by the expression of a highly active modified version of the human β1,4-galactosyltransferase in glycoengineered plants lacking plant-specific glycosylation. Moreover, we demonstrate that two anti-human immunodeficiency virus mAbs with fully β1,4-galactosylated N-glycans display improved virus neutralization potency when compared with other glycoforms produced in plants and Chinese hamster ovary cells. These findings indicate that mAbs containing such homogeneous N-glycan structures should display improved in vivo activities. Our system, using expression of mAbs in tobacco plants engineered for post-translational protein processing, provides a new means of overcoming the two hurdles that limit the therapeutic use of anti-human immunodeficiency virus mAbs in global health initiatives, low biological potency and high production costs. |
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| AbstractList | It is well established that proper N-glycosylation significantly influences the efficacy of monoclonal antibodies (mAbs). However, the specific immunological relevance of individual mAb-associated N-glycan structures is currently largely unknown, because of the heterogeneous N-glycan profiles of mAbs when produced in mammalian cells. Here we report on the generation of a plant-based expression platform allowing the efficient production of mAbs with a homogeneous β1,4-galactosylated N-glycosylation structure, the major N-glycan species present on serum IgG. This was achieved by the expression of a highly active modified version of the human β1,4-galactosyltransferase in glycoengineered plants lacking plant-specific glycosylation. Moreover, we demonstrate that two anti-human immunodeficiency virus mAbs with fully β1,4-galactosylated N-glycans display improved virus neutralization potency when compared with other glycoforms produced in plants and Chinese hamster ovary cells. These findings indicate that mAbs containing such homogeneous N-glycan structures should display improved in vivo activities. Our system, using expression of mAbs in tobacco plants engineered for post-translational protein processing, provides a new means of overcoming the two hurdles that limit the therapeutic use of anti-human immunodeficiency virus mAbs in global health initiatives, low biological potency and high production costs. It is well established that proper N -glycosylation significantly influences the efficacy of monoclonal antibodies (mAbs). However, the specific immunological relevance of individual mAb-associated N -glycan structures is currently largely unknown, because of the heterogeneous N -glycan profiles of mAbs when produced in mammalian cells. Here we report on the generation of a plant-based expression platform allowing the efficient production of mAbs with a homogeneous β1,4-galactosylated N -glycosylation structure, the major N -glycan species present on serum IgG. This was achieved by the expression of a highly active modified version of the human β1,4-galactosyltransferase in glycoengineered plants lacking plant-specific glycosylation. Moreover, we demonstrate that two anti-human immunodeficiency virus mAbs with fully β1,4-galactosylated N -glycans display improved virus neutralization potency when compared with other glycoforms produced in plants and Chinese hamster ovary cells. These findings indicate that mAbs containing such homogeneous N -glycan structures should display improved in vivo activities. Our system, using expression of mAbs in tobacco plants engineered for post-translational protein processing, provides a new means of overcoming the two hurdles that limit the therapeutic use of anti-human immunodeficiency virus mAbs in global health initiatives, low biological potency and high production costs. |
| Author | Kunert, Renate Quendler, Heribert Steinkellner, Herta Stadlmann, Johannes Mach, Lukas Jez, Jakub Rademacher, Thomas Strasser, Richard Castilho, Alexandra Altmann, Friedrich Gattinger, Pia |
| Author_xml | – sequence: 1 givenname: Richard surname: Strasser fullname: Strasser, Richard organization: Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 2 givenname: Alexandra surname: Castilho fullname: Castilho, Alexandra organization: Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 3 givenname: Johannes surname: Stadlmann fullname: Stadlmann, Johannes organization: Department of Chemistry, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 4 givenname: Renate surname: Kunert fullname: Kunert, Renate organization: Institute of Applied Microbiology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 5 givenname: Heribert surname: Quendler fullname: Quendler, Heribert organization: Polymun Scientific GmbH, 1190 Vienna, Austria – sequence: 6 givenname: Pia surname: Gattinger fullname: Gattinger, Pia organization: Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 7 givenname: Jakub surname: Jez fullname: Jez, Jakub organization: Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 8 givenname: Thomas surname: Rademacher fullname: Rademacher, Thomas organization: Rheinisch-Westfälische Technische Hochschule, 52074 Aachen, Germany – sequence: 9 givenname: Friedrich surname: Altmann fullname: Altmann, Friedrich organization: Department of Chemistry, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 10 givenname: Lukas surname: Mach fullname: Mach, Lukas organization: Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria – sequence: 11 givenname: Herta surname: Steinkellner fullname: Steinkellner, Herta email: herta.steinkellner@boku.ac.at organization: Department of Applied Genetics and Cell Biology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria |
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| SubjectTerms | Glycobiology and Extracellular Matrices |
| Title | Improved Virus Neutralization by Plant-produced Anti-HIV Antibodies with a Homogeneous β1,4-Galactosylated N-Glycan Profile |
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