Photoactivation of toxin conjugates

A novel photocleavable protein cross-linking reagent has been used for conjugation of the ribosome-inactivating protein pokeweed antiviral protein from seeds of Phytolacca americana (PAP-S), with either the monoclonal antibody 5E9 directed against the human transferrin-receptor or the B-chain of ric...

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Bibliographic Details
Published in:Bioconjugate chemistry 1992-03, Vol.3 (2), p.104-107
Main Authors: Goldmacher, Victor S, Senter, Peter D, Lambert, John M, Blattler, Walter A
Format: Article
Language:English
Subjects:
Antibodies, Monoclonal - chemistry
Biological and medical sciences
Biotechnology
Cell Survival - drug effects
Cross-Linking Reagents - chemistry
Fundamental and applied biological sciences. Psychology
Health. Pharmaceutical industry
HeLa Cells
Humans
Immunotoxins - chemistry
Immunotoxins - toxicity
Industrial applications and implications. Economical aspects
N-Glycosyl Hydrolases
Plant Proteins - chemistry
Plant Proteins - toxicity
Receptors, Transferrin - immunology
Ribosome Inactivating Proteins, Type 1
Ribosomes - drug effects
Ricin - chemistry
Ultraviolet Rays
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Summary:A novel photocleavable protein cross-linking reagent has been used for conjugation of the ribosome-inactivating protein pokeweed antiviral protein from seeds of Phytolacca americana (PAP-S), with either the monoclonal antibody 5E9 directed against the human transferrin-receptor or the B-chain of ricin that binds to cell-surface oligosaccharides bearing terminal D-galactose residues. When irradiated with near-UV light (350 nm), the linker of these conjugates undergoes photolytic degradation, resulting in the release of native toxin that is fully functional. The cytotoxicities of these 5E9-PAP-S and ricin B-chain-PAP-S conjugates for HeLa cells could be enhanced by irradiating the cells with light after they had internalized the conjugates.
ISSN:1043-1802
1520-4812
DOI:10.1021/bc00014a003