| pubmed-article:21185050 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C0949920 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C1519640 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C1554124 | lld:lifeskim |
| pubmed-article:21185050 | lifeskim:mentions | umls-concept:C0205088 | lld:lifeskim |
| pubmed-article:21185050 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21185050 | pubmed:dateCreated | 2011-1-28 | lld:pubmed |
| pubmed-article:21185050 | pubmed:abstractText | The protruding (P) domain of norovirus VP1 is responsible for immune recognition and host receptor interaction. Our previous studies have demonstrated that a modification of the ends of the P domain affects the conformation and/or function of the P protein. An expression of the P domain with or without the hinge, or with an additional cysteine at either ends of the P protein resulted in P dimers and/or P particles. Here we report a new type of subviral particle, the small P particles, through a further modification, either an addition of the flag tag or a change of the arginine cluster, at the C-terminus of the cysteine-containing P domain. Gel filtration and cryo-EM studies showed that the small P particles are tetrahedrons formed by 6 P dimers or 12 P monomers that is half-size of the P particles. Fitting of the crystal structure of the P domain into the cryo-EM density map of the particle indicated similar conformations of the P dimers as those in P particles. The small P particles bind human HBGAs and are antigenically reactive similar to their parental VLPs and P particles. These data suggest that the C-terminus of the P domain is an important factor in the formation of the P particles. Further elucidation of the mechanism of these modifications in the P particle formation would be important in structure biology and morphogenesis of noroviruses. The small P particles may also be a useful alternative in study of norovirus-host interaction and vaccine development for noroviruses. | lld:pubmed |
| pubmed-article:21185050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21185050 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21185050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21185050 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21185050 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:21185050 | pubmed:issn | 1096-0341 | lld:pubmed |
| pubmed-article:21185050 | pubmed:author | pubmed-author:JiangXiX | lld:pubmed |
| pubmed-article:21185050 | pubmed:author | pubmed-author:TanMingM | lld:pubmed |
| pubmed-article:21185050 | pubmed:author | pubmed-author:JiangWenW | lld:pubmed |
| pubmed-article:21185050 | pubmed:author | pubmed-author:XiaMingM | lld:pubmed |
| pubmed-article:21185050 | pubmed:author | pubmed-author:ChachiyoTeepa... | lld:pubmed |
| pubmed-article:21185050 | pubmed:author | pubmed-author:FangPing-AnPA | lld:pubmed |
| pubmed-article:21185050 | pubmed:copyrightInfo | Copyright © 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21185050 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21185050 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:21185050 | pubmed:volume | 410 | lld:pubmed |
| pubmed-article:21185050 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21185050 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21185050 | pubmed:pagination | 345-52 | lld:pubmed |
| pubmed-article:21185050 | pubmed:dateRevised | 2011-3-29 | lld:pubmed |
| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
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| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
| pubmed-article:21185050 | pubmed:meshHeading | pubmed-meshheading:21185050... | lld:pubmed |
| pubmed-article:21185050 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21185050 | pubmed:articleTitle | Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles. | lld:pubmed |
| pubmed-article:21185050 | pubmed:affiliation | Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229-3039, USA. | lld:pubmed |
| pubmed-article:21185050 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21185050 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21185050 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21185050 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
