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.
Original language | English (US) |
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Pages (from-to) | 714-716 |
Number of pages | 3 |
Journal | Science |
Volume | 268 |
Issue number | 5211 |
State | Published - May 5 1995 |
Externally published | Yes |
ASJC Scopus subject areas
- General