【摘 要】
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In order to investigate the prompt conformations of swine major histocompatibility complex (MHC),a swine MHC-II protein complex (SLA-II) was reconstructed in vi
【机 构】
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Bioengineering College,Dalian University,Dalian 116622,China“,”College of Veterinary Medicine,China
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In order to investigate the prompt conformations of swine major histocompatibility complex (MHC),a swine MHC-II protein complex (SLA-II) was reconstructed in vitro.DRA and DRB were cloned from a crossbred commercial pig (Changbai-Dalan).Subcloned extracellular parts of DRA and DRB were linked together by a linker containing rich glycine/serine (G4S)3,and the whole length of two genes,named DRA-linker-DRB,was amplified by splicing overlap extension PCR (SOE PCR).DRA-linker-DRB was inserted into pMAL-p2X prokaryotic system and expressed.The expressed fusion protein MBP-DRA-(G4S)3-DRB was identified by Weste-blot,purified and cleaved to obtain the protein of interest DRA-(G4S)3-DRB.The secondary structure of this protein was determined in circular dichroism (CD) apparatus.The results indicated that the subsequent protein MBP-DRA-(G4S)3-DRB was soluble and its molecule weight was 83.4 ku in consistent with the Weste-blot.Cleaved by Factor Xa,the protein of interest was separated with a molecular weight of 40.9 ku.The CD spectrum demonstrated that the protein displayed a favorable α-Helix structure,and the contents of α-Helix,β-sheet,tu,and random coil were 80 aa,121 aa,101 aa and 80 aa respectively.The identical ratios of α-Helix,β-sheet,tu,and random coil between MBP-DRA-(G4S)3-DRB and DRA-(G4S)3-DRB were 95%,96.7%,91.1% and 93.0%,respectively.The results also suggested that the reconstructed SLA-II complex presented an ideal conformation and can be used for studying its structure and function in vitro.
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