2rdh: Difference between revisions

Revision as of 19:46, 21 February 2008

Crystal structure of Staphylococcal Superantigen-Like protein 11

OverviewOverview

Staphylococcus aureus is a major pathogen that produces a family of 14 staphylococcal superantigen-like (SSL) proteins, which are structurally similar to superantigens but do not stimulate T cells. SSL11 is one member of the family that is found in all staphylococcal strains. Recombinant SSL11 bound to granulocytes and monocytes through a sialic acid-dependent mechanism and was rapidly internalized. SSL11 also bound to sialic acid-containing glycoproteins, such as the Fc receptor for IgA (FcalphaRI) and P-selectin glycoprotein ligand-1 (PSGL-1), and inhibited neutrophil attachment to a P-selectin-coated surface. Biosensor analysis of two SSL11 alleles binding to sialyl Lewis X [sLe(x)- Neu5Acalpha2-3Galbeta1-4(Fuc1-3)GlcNAc] coupled to bovine serum albumin gave dissociation constants of 0.7 and 7 mum respectively. Binding of SSL11 to a glycan array revealed specificity for glycans containing the trisaccharide sialyllactosamine (sLacNac - Neu5Acalpha2-3Galbeta1-4GlcNAc). A 1.6 A resolution crystal structure of SSL11 complexed with sLe(x) revealed a discrete binding site in the C-terminal beta-grasp domain, with predominant interactions with the sialic acid and galactose residues. A single amino acid mutation in the carbohydrate binding site abolished all SSL11 binding. Thus, SSL11 is a staphylococcal protein that targets myeloid cells by binding sialyllactosamine-containing glycoproteins.

About this StructureAbout this Structure

2RDH is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition., Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD, Mol Microbiol. 2007 Dec;66(6):1342-55. PMID:18045383

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@@ Line 4: / Line 4: @@
 ==Overview==
-Staphylococcus aureus is a major pathogen that produces a family of 14, staphylococcal superantigen-like (SSL) proteins, which are structurally, similar to superantigens but do not stimulate T cells. SSL11 is one member, of the family that is found in all staphylococcal strains. Recombinant, SSL11 bound to granulocytes and monocytes through a sialic acid-dependent, mechanism and was rapidly internalized. SSL11 also bound to sialic, acid-containing glycoproteins, such as the Fc receptor for IgA (FcalphaRI), and P-selectin glycoprotein ligand-1 (PSGL-1), and inhibited neutrophil, attachment to a P-selectin-coated surface. Biosensor analysis of two SSL11, alleles binding to sialyl Lewis X [sLe(x)-, Neu5Acalpha2-3Galbeta1-4(Fuc1-3)GlcNAc] coupled to bovine serum albumin, gave dissociation constants of 0.7 and 7 mum respectively. Binding of, SSL11 to a glycan array revealed specificity for glycans containing the, trisaccharide sialyllactosamine (sLacNac -, Neu5Acalpha2-3Galbeta1-4GlcNAc). A 1.6 A resolution crystal structure of, SSL11 complexed with sLe(x) revealed a discrete binding site in the, C-terminal beta-grasp domain, with predominant interactions with the, sialic acid and galactose residues. A single amino acid mutation in the, carbohydrate binding site abolished all SSL11 binding. Thus, SSL11 is a, staphylococcal protein that targets myeloid cells by binding, sialyllactosamine-containing glycoproteins.
+Staphylococcus aureus is a major pathogen that produces a family of 14 staphylococcal superantigen-like (SSL) proteins, which are structurally similar to superantigens but do not stimulate T cells. SSL11 is one member of the family that is found in all staphylococcal strains. Recombinant SSL11 bound to granulocytes and monocytes through a sialic acid-dependent mechanism and was rapidly internalized. SSL11 also bound to sialic acid-containing glycoproteins, such as the Fc receptor for IgA (FcalphaRI) and P-selectin glycoprotein ligand-1 (PSGL-1), and inhibited neutrophil attachment to a P-selectin-coated surface. Biosensor analysis of two SSL11 alleles binding to sialyl Lewis X [sLe(x)- Neu5Acalpha2-3Galbeta1-4(Fuc1-3)GlcNAc] coupled to bovine serum albumin gave dissociation constants of 0.7 and 7 mum respectively. Binding of SSL11 to a glycan array revealed specificity for glycans containing the trisaccharide sialyllactosamine (sLacNac - Neu5Acalpha2-3Galbeta1-4GlcNAc). A 1.6 A resolution crystal structure of SSL11 complexed with sLe(x) revealed a discrete binding site in the C-terminal beta-grasp domain, with predominant interactions with the sialic acid and galactose residues. A single amino acid mutation in the carbohydrate binding site abolished all SSL11 binding. Thus, SSL11 is a staphylococcal protein that targets myeloid cells by binding sialyllactosamine-containing glycoproteins.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Baker, E.N.]]
+[[Category: Baker, E N.]]
 [[Category: Baker, H.]]
-[[Category: Chung, M.C.]]
+[[Category: Chung, M C.]]
-[[Category: Fraser, J.D.]]
+[[Category: Fraser, J D.]]
-[[Category: Langley, R.J.]]
+[[Category: Langley, R J.]]
-[[Category: Wines, B.D.]]
+[[Category: Wines, B D.]]
 [[Category: NA]]
 [[Category: PO4]]
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 [[Category: toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:35:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:46:26 2008''