Structural highlights
Publication Abstract from PubMed
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.
Structure of Staphylococcal Enterotoxin N: Implications for Binding Properties to Its Cellular Proteins.,Zeng C, Liu Z, Han Z Int J Mol Sci. 2019 Nov 25;20(23). pii: ijms20235921. doi: 10.3390/ijms20235921. PMID:31775346[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zeng C, Liu Z, Han Z. Structure of Staphylococcal Enterotoxin N: Implications for Binding Properties to Its Cellular Proteins. Int J Mol Sci. 2019 Nov 25;20(23). pii: ijms20235921. doi: 10.3390/ijms20235921. PMID:31775346 doi:http://dx.doi.org/10.3390/ijms20235921
