Production of a fusion protein consisting of the enterotoxigenic Escherichia coli heat-labile toxin B subunit and a tuberculosis antigen in Arabidopsis thaliana

• Published in: Plant cell reports Vol. 22; no. 7; pp. 502 - 508
• Main Authors: Rigano, M M, Alvarez, M L, Pinkhasov, J, Jin, Y, Sala, F, Arntzen, C J, Walmsley, A M
• Format: Journal Article
• Language: English
• Published: Germany Springer Nature B.V 01.02.2004
• Subjects: Amino Acid Sequence; Antigens, Bacterial - biosynthesis; Antigens, Bacterial - genetics; Antigens, Bacterial - isolation & purification; Arabidopsis - genetics; Arabidopsis thaliana; Bacteria; Bacterial Proteins; Bacterial Toxins - biosynthesis; Bacterial Toxins - chemistry; Bacterial Toxins - genetics; Bacterial Toxins - isolation & purification; Base Sequence; DNA, Recombinant - genetics; E coli; Enterotoxins - biosynthesis; Enterotoxins - chemistry; Enterotoxins - genetics; Enterotoxins - isolation & purification; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Escherichia coli Proteins; Freeze Drying; ganglioside GM1; Immune system; Molecular Sequence Data; Plants, Genetically Modified; Protein Subunits; Proteins; Recombinant Fusion Proteins - biosynthesis; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - isolation & purification; Toxins; Transgenic plants; Tuberculosis; Tuberculosis Vaccines - genetics; Tuberculosis Vaccines - immunology; Tuberculosis Vaccines - isolation & purification; Vaccines, Edible - genetics; Vaccines, Edible - immunology; Vaccines, Edible - isolation & purification
• ISSN: 0721-7714; 1432-203X
• DOI: 10.1007/s00299-003-0718-2

Transgenic plants are potentially safe and inexpensive vehicles to produce and mucosally deliver protective antigens. However, the application of this technology is limited by the poor response of the immune system to non-particulate, subunit vaccines. Co-delivery of therapeutic proteins with carrier proteins could increase the effectiveness of the antigen. This paper reports the ability of transgenic Arabidopsis thaliana plants to produce a fusion protein consisting of the B subunit of the Escherichia coli heat-labile enterotoxin and a 6 kDa tuberculosis antigen, the early secretory antigenic target ESAT-6. Both components of the fusion protein were detected using GM1-ganglioside-dependent enzyme-linked immunosorbant assay. This suggested the fusion protein retained both its native antigenicity and the ability to form pentamers.