Bioactivity of the Recombinant Staphylococcal Enterotoxin Q and Its Structure Relationship Analysis

doi:10.7668/hbnxb.2010.05.017

Abstract

Abstract: The bioactivity and the structure relationship of the new kind Staphylococcal Enterotoxin Q were analyzed,and the function sits related to the superantigen activity were predicated in this study,by the methods of prokaryotic expression,affinity purification,western-blot,MTT colorimetry and homology modeling. The results showed that the rate of the expression of the purified recombinant protein GST-SEQ and His-SEQ was at 20% and 25% level of the whole protein in host cells,respectively,and the two recombined fusion protein both had good immunogenicity and the ability to induced proliferation of mouse spleen cells. The α-helices,β-strands and random coils of the SEQ mature peptide were about 32,68,116 amino acid resides,respectively,and the potential binding sits in SEQ with MHCⅡ Vβ chain were H169,H207,D209,while the binding domain with TCR was α3-β8 loop. The recombine Staphylococcus enterotoxin Q present a superantigen activity which was relate with its structure domain binding with MHCⅡVβ chain and TCR of mouse spleen cells.

Key words: Staphylococcus, Enterotoxin Q( SEQ), Expression, Bioactivity, Structural analysis

CLC Number:

Q936

ZENG Linjiao, HUANG Jinhai, LIU Ying, ZHUANG Shiwen, XUE Zhaohui. Bioactivity of the Recombinant Staphylococcal Enterotoxin Q and Its Structure Relationship Analysis[J]. ACTA AGRICULTURAE BOREALI-SINICA, 2010, 25(5): 80-84. doi: 10.7668/hbnxb.2010.05.017.

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http://www.hbnxb.net/EN/Y2010/V25/I5/80

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