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==Recombinant Alfalfa Mosaic virus coat protein virus-like particle (rAMV-CP VLP)==
<StructureSection load='7epp' size='340' side='right'caption='[[7epp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EPP 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]] 2.4&#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=7epp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7epp OCA], [https://pdbe.org/7epp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7epp RCSB], [https://www.ebi.ac.uk/pdbsum/7epp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7epp ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
VLPs are virus-like particles that comprise viral capsid proteins that can self-assemble and mimic the shape and size of real viral particles; however, because they do not contain genetic material they cannot infect host cells. VLPs have great potential as safe drug/vehicle candidates; therefore, they are gaining popularity in the field of preventive medicine and therapeutics. Indeed, extensive studies are underway to examine their role as carriers for immunization and as vehicles for delivery of therapeutic agents. Here, we examined the possibility of developing VLP-utilizing technology based on an efficient VLP production process and high-resolution structural analysis. Nicotiana benthamiana was used as an expression platform to produce the coat protein of the alfalfa mosaic virus (AMV-CP). About 250 mg/kg of rAMV-CP was produced from Nicotiana benthamiana leaves. Structural analysis revealed that the oligomeric status of rAMV-CP changed according to the composition and pH of the buffer. Size exclusion chromatography and electron microscopy analysis confirmed the optimal conditions for rAMV-CP VLP formation, and a 2.4 A resolution structure was confirmed by cryo-EM analysis. Based on the efficient protein production, VLP manufacturing technology, and high-resolution structure presented herein, we suggest that rAMV-CP VLP is a useful platform for development of various new drugs.

Characterization of alfalfa mosaic virus capsid protein using Cryo-EM.,Jeong H, Park Y, Song S, Min K, Woo JS, Lee YH, Sohn EJ, Lee S Biochem Biophys Res Commun. 2021 Jun 25;559:161-167. doi:, 10.1016/j.bbrc.2021.04.060. Epub 2021 May 1. PMID:33940388<ref>PMID:33940388</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Jeong H]]
[[Category: Lee S]]