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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-6-6
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pubmed:abstractText |
The Spike (S) protein from a virulent British field isolate of porcine transmissible gastroenteritis virus (TGEV) FS772/70 was constructed from cDNA and inserted into the vaccinia virus (VV) thymidine kinase gene locus under the control of the VV early/late gene P7.5k promoter. Recombinant S protein was synthesized as an endo-beta-N-acetylglucosaminidase H (Endo H)-sensitive glycoprotein with high mannose simple oligosaccharides (gp 190) that underwent post-translational modification to an Endo H-resistant glycoprotein with complex oligosaccharides (gp210). Immunofluorescence analysis demonstrated that the majority of recombinant S protein was retained at the Golgi but some S protein was expressed on the plasma membrane. Monoclonal antibodies (mAbs) raised against native S protein reacted with this recombinant S protein; also, mice infected with the recombinant vaccinia virus (rVV) expressing the S protein induced TGEV neutralizing antibodies. A truncated S protein (S delta) was also expressed in rVV-infected cells by introducing a deletion into the S protein cDNA that removed 292 amino acids from the C-terminus. The S delta protein (gp 170) was shown to be antigenically similar to TGEV S protein by immunofluorescence and immunoprecipitation tests but was retained in the endoplasmic reticulum and not expressed on the cell surface.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Structural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/spike protein S, Transmissible...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
182
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pubmed:geneSymbol |
S
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
765-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1850927-Amino Acid Sequence,
pubmed-meshheading:1850927-Animals,
pubmed-meshheading:1850927-Antigens, Viral,
pubmed-meshheading:1850927-Base Sequence,
pubmed-meshheading:1850927-Biological Transport,
pubmed-meshheading:1850927-Cell Compartmentation,
pubmed-meshheading:1850927-Cell Line,
pubmed-meshheading:1850927-DNA,
pubmed-meshheading:1850927-Genes, Viral,
pubmed-meshheading:1850927-Glycosylation,
pubmed-meshheading:1850927-Humans,
pubmed-meshheading:1850927-Molecular Sequence Data,
pubmed-meshheading:1850927-Protein Processing, Post-Translational,
pubmed-meshheading:1850927-Recombinant Proteins,
pubmed-meshheading:1850927-Restriction Mapping,
pubmed-meshheading:1850927-Swine,
pubmed-meshheading:1850927-Transmissible gastroenteritis virus,
pubmed-meshheading:1850927-Vaccinia virus,
pubmed-meshheading:1850927-Viral Proteins,
pubmed-meshheading:1850927-Viral Structural Proteins
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pubmed:year |
1991
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pubmed:articleTitle |
Intracellular processing of the porcine coronavirus transmissible gastroenteritis virus spike protein expressed by recombinant vaccinia virus.
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pubmed:affiliation |
Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, United Kingdom.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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