Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-6-6
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
182
pubmed:geneSymbol
S
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
765-73
pubmed:dateRevised
2006-11-15
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
pubmed:year
1991
pubmed:articleTitle
Intracellular processing of the porcine coronavirus transmissible gastroenteritis virus spike protein expressed by recombinant vaccinia virus.
pubmed:affiliation
Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, United Kingdom.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't