Abstract:
:Primate complement receptor type 1 (CR1) protein, a single-chain transmembrane glycoprotein, plays an important role in immune adherence and clearing complement-opsonized immune complexes. Here, the mRNA of the porcine primate-like complement receptor (CR1-like) gene was analyzed, and two domain sequences with potential functions were cloned into the pwPICZalpha vector for expression in Pichia pastoris. The recombinant proteins were purified with both Protein Pure Ni-NTA resin and strong anion exchange resin. The activities of the purified recombinant proteins were evaluated by SDS-PAGE, western blotting, and complement receptor assays. The results indicated that two domains of the CR1-like protein, CCP36 and CCP811 with molecular weights of 29.8 kDa and 30 kDa, respectively, were successfully expressed in P. pastoris. These two recombinant proteins possess some of the functions of the primate CR1 protein. Using these two proteins coupled with an antibody blocking technique, we also showed that CR1-like is expressed on natural porcine erythrocytes.
journal_name
Immunol Resjournal_title
Immunologic researchauthors
Yin W,Wei X,Jiang J,Fan K,Zhao J,Sun N,Wang Z,Sun Y,Ma H,Zhao X,Li Hdoi
10.1007/s12026-016-8792-zsubject
Has Abstractpub_date
2016-08-01 00:00:00pages
1025-32issue
4eissn
0257-277Xissn
1559-0755pii
10.1007/s12026-016-8792-zjournal_volume
64pub_type
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