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rdf:type |
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lifeskim:mentions |
umls-concept:C0004561,
umls-concept:C0014644,
umls-concept:C0017968,
umls-concept:C0221908,
umls-concept:C0542341,
umls-concept:C0596311,
umls-concept:C1156306,
umls-concept:C1330957,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2009-2-16
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pubmed:abstractText |
Glycoprotein B (gB) homologues within the herpesvirus family display high sequence conservation, and a number of gB homologues contain a cleavage motif R-X-K/R-R recognized by the cellular protease furin. Epstein-Barr virus (EBV) gB contains this motif and cleaved gB is found in EBV virions. To determine the functional significance of this cleavage motif in EBV gB, a deletion mutant (gB Deltafurin) was created lacking the motif. This cleavage mutant was expressed well in cell culture but was not cleaved. Experiments examining gB Deltafurin in a cell-fusion assay revealed that fusion was reduced by 52 % in epithelial and 28 % in B cells when compared with wild-type EBV gB. This decrease in cell-cell fusion is similar to that observed with multiple alphaherpesvirus gB cleavage mutants and supports a conserved function for cleaved gB.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-10725194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-11078764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-11773401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-11882994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-12970403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-15140992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-15507709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-15534216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-15583133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-16160168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-16973550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-17459936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-17554016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-17655906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-1845824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2157039,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2157862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2159568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2426466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2535741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2543773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2544666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-2556845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-3027378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-3029988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-6092679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-6266278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-6286417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-7726996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-7952927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-8107227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-89099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-9344919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-9557727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19218203-9779457
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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 |
Mar
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pubmed:issn |
0022-1317
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
591-5
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:19218203-Amino Acid Sequence,
pubmed-meshheading:19218203-Animals,
pubmed-meshheading:19218203-B-Lymphocytes,
pubmed-meshheading:19218203-Cell Fusion,
pubmed-meshheading:19218203-Epithelial Cells,
pubmed-meshheading:19218203-Gene Deletion,
pubmed-meshheading:19218203-Herpesvirus 4, Human,
pubmed-meshheading:19218203-Humans,
pubmed-meshheading:19218203-Membrane Fusion,
pubmed-meshheading:19218203-Molecular Sequence Data,
pubmed-meshheading:19218203-Mutagenesis, Site-Directed,
pubmed-meshheading:19218203-Viral Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells.
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pubmed:affiliation |
Department of Microbiology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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