Linked Life Data

7778290

Source:http://linkedlifedata.com/resource/pubmed/id/7778290

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-7-11
pubmed:abstractText
Human cytomegalovirus (HCMV) glycoprotein B (gB) promotes virion entry into cells by fusing the virion envelope with the cellular membrane. We recently reported that UB cells (U373 glioblastoma cells constructed to produce HCMV gB constitutively) form multinucleate syncytia that are dependent on the density of gB in the plasma membrane. In this report, we describe the properties of a clonal cell line, UB31-B3, that expressed a spontaneously mutated form of gB which lacked the fusion-inducing function of the wild-type molecule, and three UB cell lines that were constructed to investigate the effect of specific mutations in gB on syncytium formation. Flow cytometry analysis with a pool of monoclonal antibodies (mAbs) showed that the UB cells contained a high density of gB, which was associated with the cell surface. Immune precipitation experiments with UB31-B3 cells showed that the mutant gB reacted with all of the mAbs to the ectodomain of gB but with none of those to the cytoplasmic carboxy terminus, and that it was 35 kDa smaller than wild-type gB. Nucleotide sequence analysis showed that a termination codon had been introduced after amino acid lysine at position 669 in the ectodomain of UB31-B3 gB, generating a truncated glycoprotein. UB31-B3 gB was not secreted into the medium and was stably anchored in the plasma membrane, which suggested that a hydrophobic stretch of amino acids from 629 to 652 in the ectodomain may serve as a membrane anchor for this truncated form. Analysis of the UB cell lines expressing deleted forms of gB showed that deletion of all or part of the cytoplasmic and transmembrane domains reduced or abolished syncytium formation. In contrast, deletion of a major neutralizing region in the ectodomain of gB did not alter syncytium formation. Results of these studies indicate that different regions of the gB molecule participate in syncytium formation.
pubmed:grant
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:day
1
pubmed:volume
209
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
580-91
pubmed:dateRevised
2008-8-26
pubmed:meshHeading
pubmed-meshheading:7778290-Antibodies, Monoclonal, pubmed-meshheading:7778290-Base Sequence, pubmed-meshheading:7778290-Cell Line, pubmed-meshheading:7778290-Cell Membrane, pubmed-meshheading:7778290-Cytomegalovirus, pubmed-meshheading:7778290-DNA Primers, pubmed-meshheading:7778290-Gene Expression, pubmed-meshheading:7778290-Genes, Viral, pubmed-meshheading:7778290-Giant Cells, pubmed-meshheading:7778290-Glioblastoma, pubmed-meshheading:7778290-Humans, pubmed-meshheading:7778290-Membrane Fusion, pubmed-meshheading:7778290-Molecular Sequence Data, pubmed-meshheading:7778290-Mutagenesis, Site-Directed, pubmed-meshheading:7778290-Phosphorylation, pubmed-meshheading:7778290-Polymerase Chain Reaction, pubmed-meshheading:7778290-Recombinant Proteins, pubmed-meshheading:7778290-Tumor Cells, Cultured, pubmed-meshheading:7778290-Viral Envelope Proteins, pubmed-meshheading:7778290-Virion
pubmed:year
1995
pubmed:articleTitle
Mutated forms of human cytomegalovirus glycoprotein B are impaired in inducing syncytium formation.
pubmed:affiliation
Division of Oral Biology, School of Dentistry, University of California San Francisco 94143-0512, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't