View source for 9cvf


==Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 9-14-18==
<StructureSection load='9cvf' size='340' side='right'caption='[[9cvf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cvf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Tulane_virus Tulane virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CVF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9cvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cvf OCA], [https://pdbe.org/9cvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cvf RCSB], [https://www.ebi.ac.uk/pdbsum/9cvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cvf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B2Y6D0_9CALI B2Y6D0_9CALI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human noroviruses (HuNoVs) are a major cause of acute gastroenteritis, contributing significantly to annual foodborne illness cases. However, studying these viruses has been challenging due to limitations in tissue culture techniques for over four decades. Tulane virus (TV) has emerged as a crucial surrogate for HuNoVs due to its close resemblance in amino acid composition and the availability of a robust cell culture system. Initially isolated from rhesus macaques in 2008, TV represents a novel Calicivirus belonging to the Recovirus genus. Its significance lies in sharing the same host cell receptor, histo-blood group antigen (HBGA), as HuNoVs. In this study, we introduce, through cryo-electron microscopy (cryo-EM), the structure of a specific TV variant (the 9-6-17 TV) that has notably lost its ability to bind to its receptor, B-type HBGA-a finding confirmed using an enzyme-linked immunosorbent assay (ELISA). These results offer a profound insight into the genetic modifications occurring in TV that are necessary for adaptation to cell culture environments. This research significantly contributes to advancing our understanding of the genetic changes that are pivotal to successful adaptation, shedding light on fundamental aspects of Calicivirus evolution.

The 2.6 A Structure of a Tulane Virus Variant with Minor Mutations Leading to Receptor Change.,Sun C, Huang P, Xu X, Vago FS, Li K, Klose T, Jiang XJ, Jiang W Biomolecules. 2024 Jan 16;14(1):119. doi: 10.3390/biom14010119. PMID:38254719<ref>PMID:38254719</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cvf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Tulane virus]]
[[Category: Jiang W]]
[[Category: Sun C]]