5u75 | pdb_00005u75

The structure of Staphylococcal Enterotoxin-like X (SElX), a Unique Superantigen

spinqualitylabelsall models 5u75, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u75 is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Ligands: FUC, GAL, NDG, PRD_900122, SIA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SELX_STAAU Plays a role in the inhibition of the host innate immune system. Inhibits phagocytosis and killing by human neutrophils by interacting with multiple neutrophil surface glycoproteins in a sialic acid-dependent manner. Publication Abstract from PubMed Staphylococcus aureus is an opportunistic pathogen that produces many virulence factors. Two major families of which are the staphylococcal superantigens (SAgs) and the Staphylococcal Superantigen-Like (SSL) exoproteins. The former are immunomodulatory toxins that induce a Vbeta-specific activation of T cells, while the latter are immune evasion molecules that interfere with a wide range of innate immune defences. The superantigenic properties of Staphylococcal enterotoxin-like X (SElX) have recently been established. We now reveal that SElX also possesses functional characteristics of the SSLs. A region of SElX displays high homology to the sialyl-lactosamine (sLacNac)-specific binding site present in a sub-family of SSLs. By analysing the interaction of SElX with sLacNac-containing glycans we show that SElX has an equivalent specificity and host cell binding range to the SSLs. Mutation of key amino acids in this conserved region affects the ability of SElX to bind to cells of myeloid origin and significantly reduces its ability to protect S. aureus from destruction in a whole blood killing (WBK) assay. Like the SSLs, SElX is up-regulated early during infection and is under the control of the S. aureus exotoxin expression (Sae) two component gene regulatory system. Additionally, the structure of SElX in complex with the sLacNac-containing tetrasaccharide sialyl Lewis X (sLeX) reveals that SElX is a unique single-domain SAg. In summary, SElX is an 'SSL-like' SAg. Staphylococcal enterotoxin-like X (SElX) is a unique superantigen with functional features of two major families of staphylococcal virulence factors.,Langley RJ, Ting YT, Clow F, Young PG, Radcliff FJ, Choi JM, Sequeira RP, Holtfreter S, Baker H, Fraser JD PLoS Pathog. 2017 Sep 7;13(9):e1006549. doi: 10.1371/journal.ppat.1006549., eCollection 2017 Sep. PMID:28880913 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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