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Production of a recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system
Author(s) -
Morassutti Carla,
De Amicis Francesca,
Skerlavaj Barbara,
Zanetti Margherita,
Marchetti Stefano
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02741-2
Subject(s) - intein , peptide , recombinant dna , antimicrobial , biochemistry , transgene , chemistry , antimicrobial peptides , fusion protein , biology , microbiology and biotechnology , gene , rna , rna splicing
Tobacco plants were engineered to express SMAP‐29, a mammalian antimicrobial peptide of innate immunity, as fusion protein with modified vacuolar membrane ATPase intein. The peptide was purified taking advantage of the intein‐mediated self‐cleaving mechanism. SMAP‐29 was immunologically detected in the chromatographic eluate and appeared tightly bound to copurified plant proteins. Electrophoretic separation under disaggregating conditions indicated that the recombinant peptide was cleaved off by intein at the expected site and an overlay gel assay demonstrated that the peptide retained antimicrobial activity. These results indicate that a modified intein expression system can be used to produce pharmaceutical peptides in transgenic plants.