Here's the abstract:
>>Published online before print June 10, 2003
Proc. Natl. Acad. Sci. USA, 10.1073/pnas.0832472100
Plant Biology
Function and glycosylation of plant-derived antiviral monoclonal antibody
Kisung Ko *, Yoram Tekoah , Pauline M. Rudd , David J. Harvey , Raymond A. Dwek , Sergei Spitsin *, Cathleen A. Hanlon , Charles Rupprecht , Bernhard Dietzschold *, Maxim Golovkin *, and Hilary Koprowski *
*Biotechnology Foundation Laboratories at Thomas Jefferson University, 1020 Locust Street, JAH, Philadelphia, PA 19107; Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom; and Rabies Section, Centers for Disease Control and Prevention, 1600 Clifton Road NE, Atlanta, GA 30333
Contributed by Hilary Koprowski, April 24, 2003
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 (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.<<
Wonder if this will awaken interest in the area sufficient to make LSBC's IP and expertise worth enough to allow it to survive.
Cheers, Tuck |
