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Review
. 2003 Sep;133(3):299-306.
doi: 10.1046/j.1365-2249.2003.02203.x.

Bacterial superantigens

T Proft  1 , J D Fraser
Affiliations
Review

Bacterial superantigens

T Proft et al. Clin Exp Immunol. 2003 Sep.
No abstract available

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Figures

Fig. 1
Fig. 1
An alignment of all streptococcal and staphylococcal superantigens based on amino acid sequence. Note that TSST-1 is a clear outlier of this group and that several clusters are formed based loosely on whether they are streptococcal or staphylococcal superantigens.
Fig. 2
Fig. 2
A comparison of the co-crystal structures of three superantigens bound to MHC class II. The first is SEB which binds to the invariant α-chain of HLA-DR out to one side [36]. The TcR interacts with both SEB and MHC class II residues. The second shows TSST-1 bound to the same chain but is positioned further over the peptide groove and interacts with peptides [37]. The third structure is SPE-C bound to the polymorphic β-chain of HLA-DR2 via a zinc atom. It sits clearly over the top of the peptide groove and prevents any interaction between the TcR and the MHC molecules [42,43].
Fig. 3
Fig. 3
A structural comparison between the superantigen TSST-1 and the non-superantigenic secreted toxin SET3 [52]. SET3 shares a two-domain structure with TSST-1 with a larger C-terminal domain of the β-grasp motif and smaller N-terminal β-barrel domain. Two main α-helices are both shared and the larger α-helix contains the highly conserved superantigen PROSITE motif K-X(2)-[LIVF]-X(4)-[LIVF]-D-X(3)-R-X(2)-L-X(5)-[LIV]-Y (PS00278).
See this image and copyright information in PMC

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