Open AccessStructural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
Author(s) -
Ivan V. Bogdanov,
Ekaterina I. Finkina,
Sergey V. Balandin,
Daria N. Melnikova,
E. A. Stukacheva,
Tatiana V. Ovchinnikova
Publication year - 2015
Publication title -
acta naturae
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 26
ISSN - 2075-8251
DOI - 10.32607/20758251-2015-7-3-65-73
Subject(s) - plant lipid transfer proteins , gene isoform , recombinant dna , epitope , chemistry , biochemistry , allergen , disulfide bond , immunoglobulin e , allergy , microbiology and biotechnology , biology , antibody , gene , immunology
The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the -helical structure. It was found that Lc-LTP1 and Lc-LTP3 possess antimicrobial activity and can bind fatty acids. Both isoforms have the ability to bind specific IgE from sera of patients with food allergies, which recognize similar epitopes of the major peach allergen Pru p 3. Both isoforms were shown to have immunological properties similar to those of other plant allergenic LTPs, but Lc-LTP3 displayed a less pronounced immunoreactivity.