Abstract
A recombinant antibody-binding protein originating from streptococcal protein G was modified with lipid in a site-directed manner by genetic engineering. The resulting lipoprotein was incorporated into the surface of liposomes by simple mixing. Immunoliposomes were then prepared by binding anti-IgG antibodies molecules onto the surface of proteoliposome via the lipid-anchored streptococcal protein G. Either small fluorophores or fluorescently labeled proteins were encapsulated into prepared immunoliposomes, and these molecular tracers could be delivered into cells whose surfaces were marked with specific antibodies.
MeSH terms
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Antibodies, Anti-Idiotypic / chemistry
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Antibodies, Anti-Idiotypic / immunology
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Antibodies, Anti-Idiotypic / metabolism*
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Bacterial Proteins / genetics
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Bacterial Proteins / immunology
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Bacterial Proteins / metabolism
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Escherichia coli
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Female
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Fluorescein-5-isothiocyanate
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Fluorescence
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Gene Expression
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Genetic Engineering / methods*
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HeLa Cells
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Humans
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Lipids / genetics
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Molecular Targeted Therapy / methods*
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / immunology
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Nerve Tissue Proteins / metabolism
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Protein Binding
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Proteolipids / chemistry
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Proteolipids / immunology
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Proteolipids / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
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Recombinant Proteins / metabolism
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Streptococcus
Substances
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Antibodies, Anti-Idiotypic
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Bacterial Proteins
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G-substrate
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Lipids
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Nerve Tissue Proteins
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Proteolipids
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Recombinant Proteins
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anti-IgG
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proteoliposomes
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Fluorescein-5-isothiocyanate