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6elc

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==Crystal Structure of O-linked Glycosylated VSG3==
==Crystal Structure of O-linked Glycosylated VSG3==
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<StructureSection load='6elc' size='340' side='right' caption='[[6elc]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
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<StructureSection load='6elc' size='340' side='right'caption='[[6elc]], [[Resolution|resolution]] 1.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6elc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ELC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6elc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ELC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6elc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elc OCA], [http://pdbe.org/6elc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6elc RCSB], [http://www.ebi.ac.uk/pdbsum/6elc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6elc ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6elc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elc OCA], [https://pdbe.org/6elc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6elc RCSB], [https://www.ebi.ac.uk/pdbsum/6elc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6elc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The African trypanosome Trypanosoma brucei spp. is a paradigm for antigenic variation, the orchestrated alteration of cell surface molecules to evade host immunity. The parasite elicits robust antibody-mediated immune responses to its variant surface glycoprotein (VSG) coat, but evades immune clearance by repeatedly accessing a large genetic VSG repertoire and 'switching' to antigenically distinct VSGs. This persistent immune evasion has been ascribed exclusively to amino-acid variance on the VSG surface presented by a conserved underlying protein architecture. We establish here that this model does not account for the scope of VSG structural and biochemical diversity. The 1.4-A-resolution crystal structure of the variant VSG3 manifests divergence in the tertiary fold and oligomeric state. The structure also reveals an O-linked carbohydrate on the top surface of VSG3. Mass spectrometric analysis indicates that this O-glycosylation site is heterogeneously occupied in VSG3 by zero to three hexose residues and is also present in other VSGs. We demonstrate that this O-glycosylation increases parasite virulence by impairing the generation of protective immunity. These data alter the paradigm of antigenic variation by the African trypanosome, expanding VSG variability beyond amino-acid sequence to include surface post-translational modifications with immunomodulatory impact.
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African trypanosomes evade immune clearance by O-glycosylation of the VSG surface coat.,Pinger J, Nesic D, Ali L, Aresta-Branco F, Lilic M, Chowdhury S, Kim HS, Verdi J, Raper J, Ferguson MAJ, Papavasiliou FN, Stebbins CE Nat Microbiol. 2018 Jul 9. pii: 10.1038/s41564-018-0187-6. doi:, 10.1038/s41564-018-0187-6. PMID:29988048<ref>PMID:29988048</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6elc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Trypanosoma brucei brucei]]
[[Category: Stebbins, C E]]
[[Category: Stebbins, C E]]

Current revision

Crystal Structure of O-linked Glycosylated VSG3

PDB ID 6elc

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