Expression, purification and interaction of human leukocyte antigen F and cluster of differentiation 8alpha homodimers.
- Author:
Kaihua LUO
1
;
Zheng FAN
;
Hongbin LI
;
Yiwei LIU
Author Information
1. Institute of Microbiology, Chinese Academic of Sciences, Beijing 100101, China.
- Publication Type:Journal Article
- MeSH:
CD8 Antigens;
biosynthesis;
genetics;
Escherichia coli;
genetics;
metabolism;
Histocompatibility Antigens Class I;
biosynthesis;
genetics;
Humans;
Mutation;
Protein Interaction Domains and Motifs;
Protein Multimerization;
Recombinant Proteins;
biosynthesis;
genetics;
isolation & purification
- From:
Chinese Journal of Biotechnology
2011;27(10):1521-1526
- CountryChina
- Language:Chinese
-
Abstract:
To obtain large quantity of human leukocyte antigen F (HLA-F) and cluster of differentiation 8alpha homodimers (CD8alphaalpha) proteins and to study their relationship, HLA-F and CD8alpha genes with rare codon in Escherichia coli were cloned using an N-terminal synonymous mutation method. High-efficiency expression protein inclusion bodies were acquired. The proteins were refolded using the dilution method and purified with gel-filtration and anion exchange chromatography. The results of gel-filtration and native-PAGE indicate that HLA-F interacts with CD8alphaalpha. This interaction may affect the binding between CD8alphaalpha and other MHC molecules to regulate immune responses. These results provide a basis for further research of HLA-F.
