A soluble recombinant form of human leucocyte antigen-G 6 (srHLA-G6)

作者：Pela, Flavia Porto; Rustiguel, Joane Kathelen; Rodrigues, Lilian Cataldi; Mendonca, Jacqueline Nakau; Andrade, Camillo Del Cistia; Lopes, Norberto Peporine; Rosa, Jose Cesar; Nonato, Maria Cristina; Favier, Benoit; Donadi, Eduardo Antonio; Dias-Baruffi, Marcelo^*

来源：Biochemical and Biophysical Research Communications, 2017, 487(1): 28-33.

DOI：10.1016/j.bbrc.2017.03.149

• Human leucocyte antigen-G6
• Recombinant protein expression
• MALD-TORTOF
• MEM-G9

Human Leucocyte Antigen-G (HLA-G) is a non classical major histocompatibility complex (MHC) molecule that through RNA splicing can encode seven isoforms which are membrane bound (-G1, -G2, -G3 and -G4) and soluble (-G5, -G6 and -G7). HLA-G is described as important immune suppressor endogenous molecule to favor maternal-fetal tolerance, transplant survival and tumor immune scape. HLA-G shows low protein variability and a unique structural complexity that is related with the expression of different isoforms followed by biochemical processes, such as, proteolytic cleavage, molecular interactions, and protein ubiquitination. Studies with HLA-G have shown difficult to assess the role of the individual isoforms. Thus, the aim of this work was to obtain a HLA-G6 recombinant form. The results indicated the production of high homogeneous preparations of soluble recombinant HLA-G6 (srHLA-G6) with molecular mass 23,603.76 Da, determined by MALD-TOF/TOF. In addition, native and denatured srHLA-G6 were detected by ELISA, using commercial monoclonal antibodies. Finally, we developed a suitable methodology to express srHLA-G6 that could contribute in structural and functional studies involving specific isoforms.

• 出版日期2017-5-20
• 单位中国地震局; 中国林业科学研究院