Function and glycosylation of plant-derived antiviral monoclonal antibody

Kisung Ko, Yoram Tekoah, Pauline M. Rudd, David J. Harvey, Raymond A. Dwekt, Sergei Spitsin, Cathleen A. Hanlon, Charles Rupprecht, Bernhard Dietzschold, Maxim Golovkin, Hilary Koprowski

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201 Scopus citations


Plant genetic engineering led to the production of plant-derived mAb (mAbP), 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 (mAbM) or human rabies Ig (HRIG). The mAbP contained mainly oligomannose type N-glycans (90%) and had no potentially antigenic α(1,3)-linked fucose residues. mAbP had a shorter half-life than mAbM. The mAbP 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.

Original languageEnglish
Pages (from-to)8013-8018
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
StatePublished - 24 Jun 2003
Externally publishedYes


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