Abstract
The binding subunit of Escherichia coli heat-labile enterotoxin (LT-B) is a highly active oral immunogen. Transgenic tobacco and potato plants were made with the use of genes encoding LT-B or an LT-B fusion protein with a microsomal retention sequence. The plants expressed the foreign peptides, both of which formed oligomers that bound the natural ligand. Mice immunized by gavage produced serum and gut mucosal anti-LT-B immunoglobulins that neutralized the enterotoxin in cell protection assays. Feeding mice fresh transgenic potato tubers also caused oral immunization.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Administration, Oral
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Amino Acid Sequence
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Animals
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Bacterial Toxins / immunology
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Bacterial Vaccines / administration & dosage*
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Bacterial Vaccines / biosynthesis*
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Base Sequence
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Enterotoxins / immunology
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Escherichia coli / immunology
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Escherichia coli Proteins*
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Nicotiana
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Plants, Genetically Modified / immunology*
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Plants, Toxic
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Protein Sorting Signals
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Recombinant Fusion Proteins / immunology
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Solanum tuberosum
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Vaccines, Synthetic / administration & dosage*
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Vaccines, Synthetic / biosynthesis*
Substances
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Bacterial Toxins
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Bacterial Vaccines
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Enterotoxins
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Escherichia coli Proteins
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Protein Sorting Signals
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Recombinant Fusion Proteins
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Vaccines, Synthetic
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SEKDEL sequence
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heat-labile enterotoxin, E coli