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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
1999-2-1
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pubmed:abstractText |
Based on sequence analysis, the protein encoded by the US5 open reading frame (ORF) of herpes simplex virus type 1 (HSV-1) was predicted to contain an N-glycosylation site and was given the designation of glycoprotein J (gJ). However, the US5 gene product has not been identified and the identity of gJ as a glycoprotein has not been confirmed. We have cloned and expressed the DNA encoding the complete sequence of the US5 ORF, using a baculovirus expression system. Western blotting, using polyclonal antibody raised against synthetic US5 peptides, revealed two major baculovirus-US5-expressed protein bands with apparent molecular weights of 16-17 and 10 kD. The recombinant US5 was found on the membrane of Spodoptera frugiperda cells and was susceptible to tunicamycin, endoglycosidase H, glycosidase F and partially resistant to endoglycosidase F. Vaccination of mice with baculovirus-expressed US5 did not induce a neutralizing antibody to HSV-1 or provide protection against lethal HSV-1 challenge. However, serum from these vaccinated mice was able to recognize US5 in purified HSV-1 virions by Western blot analyses and on the surface of HSV-1-infected cells by immunofluorescence. These findings establish that US5 does encode a glycoprotein and confirm the appropriateness of naming the US5 gene product gJ.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein J, herpesvirus simiae
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pubmed:status |
MEDLINE
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pubmed:issn |
0300-5526
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
91-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9820842-Amino Acid Sequence,
pubmed-meshheading:9820842-Animals,
pubmed-meshheading:9820842-Antibodies, Viral,
pubmed-meshheading:9820842-Cell Line,
pubmed-meshheading:9820842-Cell Membrane,
pubmed-meshheading:9820842-Cloning, Molecular,
pubmed-meshheading:9820842-Genes, Viral,
pubmed-meshheading:9820842-Herpesvirus 1, Human,
pubmed-meshheading:9820842-Humans,
pubmed-meshheading:9820842-Immunization,
pubmed-meshheading:9820842-Mice,
pubmed-meshheading:9820842-Mice, Inbred BALB C,
pubmed-meshheading:9820842-Molecular Sequence Data,
pubmed-meshheading:9820842-Neutralization Tests,
pubmed-meshheading:9820842-Nucleopolyhedrovirus,
pubmed-meshheading:9820842-Open Reading Frames,
pubmed-meshheading:9820842-Rabbits,
pubmed-meshheading:9820842-Recombinant Proteins,
pubmed-meshheading:9820842-Spodoptera,
pubmed-meshheading:9820842-Viral Envelope Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
The US5 open reading frame of herpes simplex virus type 1 does encode a glycoprotein (gJ).
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pubmed:affiliation |
Ophthalmology Research, Cedars-Sinai Medical Center Research Institute, Los Angeles, Calif., 90048, USA. ghiasi@csmc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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