Glyoxalase I activity has been shown to be directly related to
cancer and its inhibitors have been used as anti-
cancer drugs. Immunochemical studies have shown immunochemical relatedness among animal and plant
glyoxalase I, but its potential application for biomedical research has not been investigated. In order to understand the conserved immunochemical regions of the
protein and to determine probable
immunomodulation targets, a
cellulose-bound scanning
peptide library for Brassica juncea
glyoxalase I was made using the spot synthesis method. Immuno-probing of the library, using B. juncea anti-
glyoxalase I monospecific polyclonal
antibodies, revealed three
immunodominant regions,
epitope I, II, and III. In the homology model of B. juncea
glyoxalase I generated by threading its sequence onto the human
glyoxalase I, the high accessible surface area and the hydrophilic nature of the
epitopes confirmed their surface localization and hence their accessibility for
antigen-antibody interaction.
Epitopes I and II were specific to B. juncea
glyoxalase I. Localizing the
epitopes on available
glyoxalase I sequences showed that
epitope III containing the active site region was conserved across phyla. Therefore, this could be used as a potential
immunomodulation target for
cancer therapy. Moreover, as the most immunogenic
epitopes were mapped on the surface of the
protein, this method could be used to discover potential therapeutic targets. It is a simple and fast approach for such investigations. This study, to our knowledge, is the first in
epitope mapping of
glyoxalase I and has great biomedical potential.