Your browser doesn't support javascript.
loading
Sequence Analysis and Biochemical Characteristics of Two Non-specific Lipid Transfer Proteins from Tartary Buckwheat Seeds.
Cui, Xiaodong; Tian, Wenhua; Wang, Wenhua; Li, Jiao; Wang, Zhuanhua; Li, Chen.
Affiliation
  • Cui X; Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Biotechnology, Shanxi University, Taiyuan, 030006, P.R. China.
  • Tian W; Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Biotechnology, Shanxi University, Taiyuan, 030006, P.R. China.
  • Wang W; Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Biotechnology, Shanxi University, Taiyuan, 030006, P.R. China.
  • Li J; School of Life Science, Shanxi University, Taiyuan, 030006, China.
  • Wang Z; School of Life Science, Shanxi University, Taiyuan, 030006, China.
  • Li C; School of Life Science, Shanxi University, Taiyuan, 030006, China.
Protein Pept Lett ; 30(6): 520-529, 2023.
Article de En | MEDLINE | ID: mdl-37171010
ABSTRACT

INTRODUCTION:

Plant non-specific lipid transfer proteins (nsLTPs) play an important role in plant resistance to various stresses, and show potential applications in agriculture, industrial manufacturing, and medicine. In addition, as more and more nsLTPs are identified as allergens, nsLTPs have attracted interest due to their allergenicity. Two nsLTPs from Tartary buckwheat have been isolated and identified. There is a need to study their biochemical characteristics and allergenicity.

OBJECTIVE:

The study aims to investigate the biochemical characteristics of two nsLTPs from Tartary buckwheat seeds and evaluate their potential allergenicity.

METHODS:

Two nsLTPs derived from Tartary buckwheat, namely FtLTP1a and FtLTP1b, were produced by gene cloning, expression, and purification. Sequence analysis and biochemical characteristics of the proteins, including lipid binding ability, α-amylase inhibition activity, antifungal activity, and allergenic activity, were investigated.

RESULTS:

High-purity recombinant FtLTP1a and FtLTP1b were obtained. FtLTP1a and FtLTP1b exhibited similar lipid binding and antifungal properties. Only FtLTP1b showed weak inhibitory activity against α-amylase.

CONCLUSION:

FtLTP1b could specifically bind IgE in the serum allergic to buckwheat and cross-react with pollen (w6). FtLTP1b is a novel allergenic member of the lipid-transfer protein 1 family found in Tartary buckwheat.
Sujet(s)
Mots clés

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Fagopyrum Type d'étude: Prognostic_studies Langue: En Journal: Protein Pept Lett Sujet du journal: BIOQUIMICA Année: 2023 Type de document: Article

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Fagopyrum Type d'étude: Prognostic_studies Langue: En Journal: Protein Pept Lett Sujet du journal: BIOQUIMICA Année: 2023 Type de document: Article