https://scholars.lib.ntu.edu.tw/handle/123456789/416903
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Tsai C.-W. | en_US |
dc.contributor.author | SHIN CHANG | en_US |
dc.contributor.author | MING-FU CHANG | en_US |
dc.creator | Tsai C.-W.;Chang, S.C.;Ming-Fu Chang | - |
dc.date.accessioned | 2019-08-30T02:32:34Z | - |
dc.date.available | 2019-08-30T02:32:34Z | - |
dc.date.issued | 1999 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033543749&doi=10.1074%2fjbc.274.37.26085&partnerID=40&md5=aa15ebd76ea5ba967f5d8d48cc370321 | - |
dc.identifier.uri | https://scholars.lib.ntu.edu.tw/handle/123456789/416903 | - |
dc.description.abstract | The spike (S) glycoprotein of mouse hepatitis virus (MHV) plays a major role in the viral pathogenesis. It is often processed into the N-terminal S1 and the C-terminal S2 subunits that were evidently important for binding to cell receptor and inducing cell-cell fusion, respectively. As a consequence of cell-cell fusion, most of the naturally occurring infections of MHV are associated with syncytia formation. So far, only MHV-2 was identified to be fusion-negative. In this study, the S gene of MHV-2 was molecularly cloned, and the nucleotide sequence was determined. The MHV-2 S protein lacks a 12- amino acid stretch in the S1 hypervariable region from amino acid residue 446 to 457 when compared with the fusion-positive strain MHV-JHM. In addition, there are three amino acid substitutions in the S2 subunit, Tyr-1144 to Asp, Glu-1165 to Asp, and Arg-1209 to Lys. The cloned MHV-2 S protein exhibited the fusion-negative property in DBT cells as the intrinsic viral protein. Furthermore, similar to the fusion-positive MHV-JHM strain, proteolytic cleavage activity was detected both in DBT cells infected with the fusion- negative MHV-2 and in the transfected cells that expressed the cloned MHV-2 S protein. Domain swapping experiments demonstrated that the 12-amino acid stretch missing in the MHV-2 S1 subunit, but not the proteolytic cleavage site, was critical for the cell-fusion activity of MHV. | en_US |
dc.language.iso | en_US | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.classification | [SDGs]SDG3 | - |
dc.subject.other | amino acid; protein subunit; virus glycoprotein; amino terminal sequence; animal cell; article; carboxy terminal sequence; cell fusion; controlled study; hepatitis virus; molecular cloning; mouse; nonhuman; nucleotide sequence; priority journal; protein degradation; receptor binding; sequence analysis; Animals; Base Sequence; Cell Fusion; Cell Line; Cloning, Molecular; DNA Primers; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Sequence Deletion; Viral Envelope Proteins; Animalia; DNA viruses; Murine hepatitis virus | - |
dc.title | A 12-amino acid stretch in the hypervariable region of the spike protein S1 subunit is critical for cell fusion activity of mouse hepatitis virus | en_US |
dc.type | journal article | en |
dc.identifier.doi | 10.1074/jbc.274.37.26085 | - |
dc.identifier.pmid | 10473557 | - |
dc.identifier.scopus | 2-s2.0-0033543749 | - |
dc.relation.pages | 26085-26090 | en_US |
dc.relation.journalvolume | 274 | en_US |
dc.relation.journalissue | 37 | en_US |
item.openairetype | journal article | - |
item.fulltext | no fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.grantfulltext | none | - |
item.languageiso639-1 | en_US | - |
item.cerifentitytype | Publications | - |
crisitem.author.dept | Microbiology | - |
crisitem.author.dept | Biochemistry and Molecular Biology | - |
crisitem.author.orcid | 0000-0002-0365-8364 | - |
crisitem.author.orcid | 0000-0001-7062-3578 | - |
crisitem.author.parentorg | College of Medicine | - |
crisitem.author.parentorg | College of Medicine | - |
顯示於: | 微生物學科所 |
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