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==Structural characterization of a GII.4 2004 norovirus variant (TCH05) bound to Secretor Lewis HBGA (LeB)==
==Structural characterization of a GII.4 2004 norovirus variant (TCH05) bound to Secretor Lewis HBGA (LeB)==
<StructureSection load='3sej' size='340' side='right' caption='[[3sej]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
<StructureSection load='3sej' size='340' side='right'caption='[[3sej]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sej]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SEJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sej]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_Hu/GII.4/2004/NL Norovirus Hu/GII.4/2004/NL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SEJ FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.041&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sej RCSB], [http://www.ebi.ac.uk/pdbsum/3sej PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<table>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sej OCA], [https://pdbe.org/3sej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sej RCSB], [https://www.ebi.ac.uk/pdbsum/3sej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sej ProSAT]</span></td></tr>
<div style="background-color:#fffaf0;">
</table>
== Publication Abstract from PubMed ==
== Function ==
Susceptibility to norovirus (NoV), a major pathogen of epidemic gastroenteritis, is associated with histo-blood group antigens (HBGAs), which are also cell attachment factors for this virus. GII.4 NoV strains are predominantly associated with worldwide NoV epidemics with a periodic emergence of new variants. The sequence variations in the surface exposed P domain of the capsid protein resulting in differential HBGA binding patterns and antigenicity are suggested to drive GII.4 epochal evolution. To understand how temporal sequence variations affect the P domain structure and contribute to epochal evolution, we determined the P domain structure of a 2004 variant with ABH and secretor Lewis HBGAs and compared it with the previously determined structure of a 1996 variant. We show that temporal sequence variations do not affect the binding of monofucosyl ABH HBGAs but they can modulate the binding strength of difucosyl Lewis HBGAs and thus could contribute to epochal evolution by potentiated targeting of new variants to Lewis-positive secretor-positive individuals. The temporal variations also result in significant differences in the electrostatic landscape likely reflecting antigenic variations. The proximity of some of these changes to the HBGA binding sites suggests the possibility of a coordinated interplay between antigenicity and HBGA binding in epochal evolution. From the observation that the regions involved in the formation of the HBGA binding sites can be conformationally flexible, we suggest a plausible mechanism for how norovirus disassociates from salivary mucin-linked HBGA before re-associating with HBGAs linked to intestinal epithelial cells during its passage through the gastrointestinal tract.
[https://www.uniprot.org/uniprot/Q5EGK8_9CALI Q5EGK8_9CALI]
 
Structural Analysis of HBGA Binding Specificity in a Norovirus GII.4 Epidemic Variant: Implications for Epochal Evolution.,Shanker S, Choi JM, Sankaran B, Atmar RL, Estes MK, Prasad BV J Virol. 2011 Jun 29. PMID:21715503<ref>PMID:21715503</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Viruses]]
[[Category: Large Structures]]
[[Category: Atmar, R L.]]
[[Category: Norovirus Hu/GII 4/2004/NL]]
[[Category: Choi, J M.]]
[[Category: Atmar RL]]
[[Category: Estes, M K.]]
[[Category: Choi J-M]]
[[Category: Prasad, B V.V.]]
[[Category: Estes MK]]
[[Category: Sankaran, B.]]
[[Category: Prasad BVV]]
[[Category: Shanker, S.]]
[[Category: Sankaran B]]
[[Category: Carbohydrate/sugar binding]]
[[Category: Shanker S]]
[[Category: Human blood group antigen]]
[[Category: Leb bound]]
[[Category: Lewis family]]
[[Category: Protein-carbohydrate complex]]
[[Category: Receptor binding]]
[[Category: Viral protein]]

Latest revision as of 09:49, 1 March 2024

Structural characterization of a GII.4 2004 norovirus variant (TCH05) bound to Secretor Lewis HBGA (LeB)

3sej, resolution 3.04Å

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