Function and glycosylation of plant-derived antiviral monoclonal antibody.

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 alpha(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.

authors

Ko K,Tekoah Y,Rudd PM,Harvey DJ,Dwek RA,Spitsin S,Hanlon CA,Rupprecht C,Dietzschold B,Golovkin M,Koprowski H

doi

10.1073/pnas.0832472100

keywords:

subject

Has Abstract

pub_date

2003-06-24 00:00:00

pages

8013-8

issue

13

eissn

0027-8424

issn

1091-6490

pii

0832472100

journal_volume

100

pub_type

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