Structure and immunomodulation activity of a novel mannose binding lectin from housefly pupae.
- Author:
Chunling WANG
1
;
Yan XIA
;
Shijiao ZHANG
;
Lirui WANG
;
Xiaohong CAO
Author Information
1. Key Laboratory of Food Nutrition and Safety, College of Food Engineering and Biotechnology, Tianjin University of Science Technology, Ministry of Education, Tianjin 300457, China. wangchunling@tust.edu.cn
- Publication Type:Journal Article
- MeSH:
Animals;
Glycoproteins;
analysis;
Houseflies;
chemistry;
Immunomodulation;
immunology;
physiology;
Macrophages;
immunology;
Mannose-Binding Lectin;
chemistry;
physiology;
Oligosaccharides;
analysis;
Pupa;
chemistry
- From:
Chinese Journal of Biotechnology
2013;29(5):601-611
- CountryChina
- Language:Chinese
-
Abstract:
We purified a novel mannose binding lectin form Musca domestica pupae by affinity chromatography on Con A-Sepharose 4B and DEAE weak anion-exchange chromatography. By SDS-PAGE, MBL-1 yielded a single band with the molecular weight of 24 kDa. It was a glycoprotein detected by periodic acid-schiffs staining reaction, with 97.36% protein and 2.1% oligosaccharide. Meanwhile, the results of beta-elimination reaction, infrared spectroscopy, atomic force microscopy and protein sequencing instrument show that MBL-1 was an ellipsoidal-shaped monomer with 60-100 nm in diameter. N-glycoside bond linked oligosaccharide chain and the N-terminal blocked peptide chain. Further study suggested that MBL-1 promote the proliferation of macrophage in a concentration-dependent manner. The scanning electron microscope analysis shows that MBL-1 promoted the activation of macrophages. These results show that MBL-1 purified from Musca domestica pupae possesses immune regulation effect, serving a reference basis to develop natural immune-modulator.
