Open AccessАffinity properties of plant-made anti-her2 antibodies
Author(s) -
A. I. Scherbakov,
Е. Н. Кособокова,
M. V. Pinyugina,
Ekaterina V. Sheshukova,
В. С. Косоруков
Publication year - 2018
Publication title -
rossijskij bioterapevtičeskij žurnal
Language(s) - English
Resource type - Journals
eISSN - 1726-9792
pISSN - 1726-9784
DOI - 10.17650/1726-9784-2018-17-1-95-100
Subject(s) - nicotiana benthamiana , monoclonal antibody , antibody , trastuzumab , recombinant dna , flow cytometry , antigen , hybridoma technology , microbiology and biotechnology , chemistry , biology , virology , biochemistry , immunology , cancer , breast cancer , virus , genetics , gene
The Her2 receptor is an important target for antitumor therapy in the treatment of breast cancer. Trastuzumab, based on anti-Her2 monoclonal antibodies, is used in clinical practice. Trastuzumab is produced by animal cells culture technology and is quite expensive. We use the technology of production of recombinant antibodies in the plants Nicotiana benthamiana with a high yield of final purified protein. Objective. The aim of following study is a comparison of monoclonal antibodies received via classic cell culture technology and produced in plant biomass. Materials and methods. Recombinant plant-made antibodies were isolated by affinity chromatography from the biomass of N. benthamiana plants agroinfiltrated by vector constructs. Comparison of affinity properties was carried out by immunocytochemical staining of cells and competitive binding using flow cytometry analysis. Results and conclusion. We show that the antibodies expressed in N. benthamiana are equal to those obtained from mammalian cells in binding to Her2 antigen localized on the surface of the SK-BR-3 cells. In the present work it was shown that the plant-made anti-Her2 antibodies do not differ in specific binding with the Her2 antigen, as well as with IV subdomain of the Her2 receptor.