| pubmed-article:19420077 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C2806455 | lld:lifeskim |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:19420077 | lifeskim:mentions | umls-concept:C0389916 | lld:lifeskim |
| pubmed-article:19420077 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:19420077 | pubmed:dateCreated | 2009-6-25 | lld:pubmed |
| pubmed-article:19420077 | pubmed:abstractText | The coronavirus nucleocapsid protein (N), together with the large, positive-strand RNA viral genome, forms a helically symmetric nucleocapsid. This ribonucleoprotein structure becomes packaged into virions through association with the carboxy-terminal endodomain of the membrane protein (M), which is the principal constituent of the virion envelope. Previous work with the prototype coronavirus mouse hepatitis virus (MHV) has shown that a major determinant of the N-M interaction maps to the carboxy-terminal domain 3 of the N protein. To explore other domain interactions of the MHV N protein, we expressed a series of segments of the MHV N protein as fusions with green fluorescent protein (GFP) during the course of viral infection. We found that two of these GFP-N-domain fusion proteins were selectively packaged into virions as the result of tight binding to the N protein in the viral nucleocapsid, in a manner that did not involve association with either M protein or RNA. The nature of each type of binding was further explored through genetic analysis. Our results defined two strongly interacting regions of the N protein. One is the same domain 3 that is critical for M protein recognition during assembly. The other is domain N1b, which corresponds to the N-terminal domain that has been structurally characterized in detail for two other coronaviruses, infectious bronchitis virus and the severe acute respiratory syndrome coronavirus. | lld:pubmed |
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| pubmed-article:19420077 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19420077 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19420077 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19420077 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19420077 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19420077 | pubmed:issn | 1098-5514 | lld:pubmed |
| pubmed-article:19420077 | pubmed:author | pubmed-author:MastersPaul... | lld:pubmed |
| pubmed-article:19420077 | pubmed:author | pubmed-author:KoetznerCheri... | lld:pubmed |
| pubmed-article:19420077 | pubmed:author | pubmed-author:HurstKelley... | lld:pubmed |
| pubmed-article:19420077 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19420077 | pubmed:volume | 83 | lld:pubmed |
| pubmed-article:19420077 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19420077 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19420077 | pubmed:pagination | 7221-34 | lld:pubmed |
| pubmed-article:19420077 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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