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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1982-8-7
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pubmed:abstractText |
We performed affinity chromatography and immunoprecipitation experiments to determine whether cells infected with herpes simplex virus type 2 (HSV-2) expressed a glycoprotein that was functionally and antigenically related to the HSV-1 Fc-binding glycoprotein designated gE. We found that a protein from extracts of HSV-2-infected HEp-2 cells bound specifically to an Fc affinity column and that the electrophoretic mobility of this protein in sodium dodecyl sulfate-acrylamide gels was slightly less than the mobility of HSV-1 gE. Immunoprecipitation experiments performed with an antiserum prepared against HSV-1 gE revealed that (i) extracts from HSV-2-infected cells contained a glycoprotein that was antigenically related to HSV-1 gE; (ii) the electrophoretic mobility of the HSV-2 gE was indistinguishable from the mobility of the HSV-2 Fc-binding protein; (iii) the antiserum reacted with both newly synthesized transient forms and stable fully processed forms of both HSV-1 gE and HSV-2 gE; and (iv) the transient and stable forms of HSV-2 gE all had lower electrophoretic mobilities than their HSV-1 counterparts. Electrophoretic analyses of gE precipitated from extracts of HEp-2 cells infected with two sets of HSV-1 x HSV-2 intertypic recombinant viruses suggested that the gene for gE is located at the right end of the HSV genome (0.85 to 0.97 map units) in the unique portion of the S component.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-1172191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-14210996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-14402487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-14493436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-198577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-214583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-219254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-219593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-229267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-357652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-4108570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-4296753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-4300104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-4348966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-4367308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-5694774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-6246278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-6247430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-6275122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6283108-6283107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-538X
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pubmed:author |
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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 |
137-44
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6283108-Antigens, Viral,
pubmed-meshheading:6283108-Genes, Viral,
pubmed-meshheading:6283108-Glycoproteins,
pubmed-meshheading:6283108-Receptors, Fc,
pubmed-meshheading:6283108-Recombination, Genetic,
pubmed-meshheading:6283108-Simplexvirus,
pubmed-meshheading:6283108-Viral Proteins,
pubmed-meshheading:6283108-Virus Replication
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pubmed:year |
1982
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pubmed:articleTitle |
Similarities and differences in the Fc-binding glycoprotein (gE) of herpes simplex virus types 1 and 2 and tentative mapping of the viral gene for this glycoprotein.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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