Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein

被引：17

作者：

Bogdanov, I. V. ^{[1
]}

Finkina, E. I. ^{[1
]}

Balandin, S. V. ^{[1
]}

Melnikova, D. N. ^{[1
]}

Stukacheva, E. A. ^{[1
]}

Ovchinnikova, T. V. ^{[1
]}

机构：

[1] Russian Acad Sci, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

来源：

ACTA NATURAE | 2015年 / 7卷 / 03期

基金：

俄罗斯基础研究基金会;

关键词：

lipid transfer protein; isoform; lentil; allergen; cross-reactivity; heterologous expression; antimicrobial activity; lipid binding; LENS-CULINARIS; ALLERGEN; EXPRESSION; PURIFICATION; EPITOPES; PLANTS; CELLS; SEEDS;

D O I：

10.32607/20758251-2015-7-3-65-73

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 a-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.

引用

页码：65 / 73

页数：9

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