1ynt
From Proteopedia
(New page: 200px<br /> <applet load="1ynt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ynt, resolution 3.100Å" /> '''Structure of the i...) |
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| - | [[Image:1ynt.gif|left|200px]]<br /> | + | [[Image:1ynt.gif|left|200px]]<br /><applet load="1ynt" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ynt" size=" | + | |
caption="1ynt, resolution 3.100Å" /> | caption="1ynt, resolution 3.100Å" /> | ||
'''Structure of the immunodominant epitope displayed by the surface antigen 1 (SAG1) of Toxoplasma gondii complexed to a monoclonal antibody'''<br /> | '''Structure of the immunodominant epitope displayed by the surface antigen 1 (SAG1) of Toxoplasma gondii complexed to a monoclonal antibody'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Toxoplasma gondii, the intracellular parasite responsible for | + | Toxoplasma gondii, the intracellular parasite responsible for toxoplasmosis infects more than one-third of the world population and can be life-threatening for fetuses and immunocompromised patients. The surface protein SAG1 is an important immune target, which provides a strong immune response against the invasive tachyzoite while the other forms of the parasite, devoid of SAG1 at their surface, are multiplying. In addition to this role as a "hot spot" decoy, SAG1 is predicted to act as an adhesin during host-cell attachment through its binding to proteoglycans. To begin to understand the relationships between SAG1 epitopes and the ligand-binding site, we have solved the crystal structure of the monomeric form of T.gondii SAG1 complexed to a Fab derived from a monoclonal antibody raised against tachyzoite particles. This antibody competes strongly with human Toxoplasma-specific sera, suggesting that its epitope is part of an immunodominant region present on the surface of SAG1. The structure reveals that this conformational epitope, located within the SAG1 N-terminal domain, does not overlap with the proposed ligand-binding pocket. This study provides the first structural description of the monomeric form of SAG1, and significant insights into its dual role of adhesin and immune target during parasite infection. |
==About this Structure== | ==About this Structure== | ||
| - | 1YNT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YNT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Battail-Poirot, N]] | [[Category: Battail-Poirot, N]] | ||
[[Category: Bossus, M.]] | [[Category: Bossus, M.]] | ||
| - | [[Category: Du, M | + | [[Category: Du, M H.Le.]] |
[[Category: Ducancel, F.]] | [[Category: Ducancel, F.]] | ||
[[Category: Graille, M.]] | [[Category: Graille, M.]] | ||
[[Category: Letourneur, O.]] | [[Category: Letourneur, O.]] | ||
| - | [[Category: Muller, B | + | [[Category: Muller, B H.]] |
[[Category: Rolland, D.]] | [[Category: Rolland, D.]] | ||
[[Category: Sibai, G.]] | [[Category: Sibai, G.]] | ||
| - | [[Category: Stura, E | + | [[Category: Stura, E A.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: conformational epitope]] | [[Category: conformational epitope]] | ||
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[[Category: toxoplasma gondii]] | [[Category: toxoplasma gondii]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:16 2008'' |
Revision as of 14:07, 21 February 2008
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Structure of the immunodominant epitope displayed by the surface antigen 1 (SAG1) of Toxoplasma gondii complexed to a monoclonal antibody
Overview
Toxoplasma gondii, the intracellular parasite responsible for toxoplasmosis infects more than one-third of the world population and can be life-threatening for fetuses and immunocompromised patients. The surface protein SAG1 is an important immune target, which provides a strong immune response against the invasive tachyzoite while the other forms of the parasite, devoid of SAG1 at their surface, are multiplying. In addition to this role as a "hot spot" decoy, SAG1 is predicted to act as an adhesin during host-cell attachment through its binding to proteoglycans. To begin to understand the relationships between SAG1 epitopes and the ligand-binding site, we have solved the crystal structure of the monomeric form of T.gondii SAG1 complexed to a Fab derived from a monoclonal antibody raised against tachyzoite particles. This antibody competes strongly with human Toxoplasma-specific sera, suggesting that its epitope is part of an immunodominant region present on the surface of SAG1. The structure reveals that this conformational epitope, located within the SAG1 N-terminal domain, does not overlap with the proposed ligand-binding pocket. This study provides the first structural description of the monomeric form of SAG1, and significant insights into its dual role of adhesin and immune target during parasite infection.
About this Structure
1YNT is a Single protein structure of sequence from Finegoldia magna, Mus musculus and Toxoplasma gondii with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the complex between the monomeric form of Toxoplasma gondii surface antigen 1 (SAG1) and a monoclonal antibody that mimics the human immune response., Graille M, Stura EA, Bossus M, Muller BH, Letourneur O, Battail-Poirot N, Sibai G, Gauthier M, Rolland D, Le Du MH, Ducancel F, J Mol Biol. 2005 Nov 25;354(2):447-58. Epub 2005 Sep 30. PMID:16242717
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