Structure of Staphylococcal Enterotoxin N: Implications for Binding Properties to Its Cellular Proteins
文献类型: 外文期刊
作者: Zeng, Chi 1 ; Liu, Zhaoxin 1 ; Han, Zhenggang 1 ;
作者机构: 1.Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan 430023, Hubei, Peoples R China
2.Wuhan Polytech Univ, Hubei Prov Fresh Food Engn Res Ctr, Wuhan 430023, Hubei, Peoples R China
3.Hubei Acad Agr Sci, Inst Anim Husb & Vet, Minist Agr, Key Lab Prevent & Control Agents Anim Bacteriosis, Wuhan 430064, Hubei, Peoples R China
4.Wuhan Univ, Coll Life Sci, Wuhan 430072, Hubei, Peoples R China
关键词: superantigens; staphylococcal enterotoxin; major histocompatibility complex class II; T-cell receptor
期刊名称:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES ( 影响因子:5.923; 五年影响因子:6.132 )
ISSN:
年卷期: 2019 年 20 卷 23 期
页码:
收录情况: SCI
摘要: Staphylococcus aureus strains produce a unique family of immunostimulatory exotoxins termed as bacterial superantigens (SAgs), which cross-link major histocompatibility complex class II (MHC II) molecule and T-cell receptor (TCR) to stimulate large numbers of T cells at extremely low concentrations. SAgs are associated with food poisoning and toxic shock syndrome. To date, 26 genetically distinct staphylococcal SAgs have been reported. This study reports the first X-ray structure of newly characterized staphylococcal enterotoxin N (SEN). SEN possesses the classical two domain architecture that includes an N-terminal oligonucleotide-binding fold and a C-terminal beta-grasp domain. Amino acid and structure alignments revealed that several critical amino acids that are proposed to be responsible for MHC II and TCR molecule engagements are variable in SEN, suggesting that SEN may adopt a different binding mode to its cellular receptors. This work helps better understand the mechanisms of action of SAgs.
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