Hepatitis B surface antigen immunopurification using a plant-derived specific antibody produced in large scale

This paper provides an evaluation of a plant-derived HBsAg-specific antibody in the immunopurification of the recombinant HBsAg for vaccine purposes. This plant-derived antibody was obtained from different batches of 100–200 kg of tobacco leaves and coupled to Sepharose CL-4B with high efficiency. T...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-10, Vol.310 (3), p.742-747
Main Authors: Valdés, Rodolfo, Reyes, Biunayki, Alvarez, Tatiana, Garcı́a, Janet, Montero, José A, Figueroa, Alejandro, Gómez, Leonardo, Padilla, Sigifredo, Geada, Déborah, Abrahantes, Ma Carmen, Dorta, Lamay, Fernández, Damián, Mendoza, Otto, Ramirez, Nadia, Rodriguez, Marylin, Pujol, Merardo, Borroto, Carlos, Brito, José
Format: Article
Language:English
Subjects:
Animals
Antibodies - chemistry
Antibodies, Monoclonal - metabolism
Antigens - metabolism
Blotting, Western
Cell Line, Tumor
Chromatography
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Hepatitis B Surface Antigens - isolation & purification
Hepatitis B Vaccines - chemistry
Hepatitis B virus
Hepatitis B virus surface antigen
Humans
Immunoaffinity
Immunoglobulin G - metabolism
Ligands
Mice
Mice, Inbred BALB C
Monoclonal antibody
Nicotiana - chemistry
Nicotiana - immunology
Plant Proteins - metabolism
Plant-derived antibody
Plants - immunology
Plants, Genetically Modified
Recombinant Proteins - chemistry
Transgenic plant
Vaccines, Synthetic - chemistry
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Summary:This paper provides an evaluation of a plant-derived HBsAg-specific antibody in the immunopurification of the recombinant HBsAg for vaccine purposes. This plant-derived antibody was obtained from different batches of 100–200 kg of tobacco leaves and coupled to Sepharose CL-4B with high efficiency. The plant-derived antibody immunoaffinity matrix purification behavior (elution capacity, antigen purity, purification cycles, and ligand leakage) was comparable to that of its mouse-derived monoclonal antibody homolog. This result supports the feasibility of using this plant-derived antibody for the immunopurification of the Hepatitis B surface antigen for human use, opening a new possibility to overcome the constrain of monoclonal antibody production in mice.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2003.08.149