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

Research output: Contribution to journalArticlepeer-review

201 Scopus citations

Abstract

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
Volume100
Issue number13
DOIs
StatePublished - 24 Jun 2003
Externally publishedYes

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