Function and glycosylation of plant-derived antiviral monoclonal antibodyopen access
- Authors
- Ko, KS; Tekoah, Y; Rudd, PM; Harvey, DJ; Dwek, RA; Spitsin, S; Hanlon, CA; Rupprecht, C; Dietzschold, B; Golovkin, M; Koprowski, H
- Issue Date
- Jun-2003
- Publisher
- NATL ACAD SCIENCES
- Citation
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.100, no.13, pp 8013 - 8018
- Pages
- 6
- Journal Title
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Volume
- 100
- Number
- 13
- Start Page
- 8013
- End Page
- 8018
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/66695
- DOI
- 10.1073/pnas.0832472100
- ISSN
- 0027-8424
1091-6490
- Abstract
- Plant genetic engineering led to the production of plant-derived mAb (mAb(P)), which provides a safe and economically feasible alternative to the current methods of antibody production in animal systems. In this study, the heavy and light chains of human anti-rabies mAb were expressed and assembled in planta under the control of two strong constitutive promoters. An alfalfa mosaic virus untranslated leader sequence and Lys-Asp-Glu-Leu (KDEL) endoplasmic reticulum retention signal were linked at the N and C terminus of the heavy chain, respectively. mAbP was as effective at neutralizing the activity of the rabies virus as the mammalian-derived antibody (mAb(M)) or human rabies Ig (HRIG). The mAb(P) contained mainly oligomannose type N-glycans (90%) and had no potentially antigenic alpha(1,3)-linked fucose residues. mAb(P) had a shorter half-life than mAb(M). The mAb(P) was as efficient as HRIG for post-exposure prophylaxis against rabies virus in hamsters, indicating that differences in N-glycosylation do not affect the efficacy of the antibody in this model.
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