Source:http://linkedlifedata.com/resource/pubmed/id/10640539
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 1
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pubmed:dateCreated |
2000-2-23
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pubmed:databankReference | |
pubmed:abstractText |
A cDNA clone encoding a partial putative human cytomegalovirus (HCMV) gH fusion receptor (CMVFR) was previously identified. In this report, the cDNA sequence of CMVFR was determined and the role of this CMVFR in HCMV/cell fusion was confirmed by rendering fusion-incompetent MOLT-4 cells susceptible to fusion following transfection with receptor cDNA. Blocking experiments using recombinant gH or either of two MAbs (against recombinant gH or purified viral gH:gL) provided additional evidence for the role of gH binding to this protein in virus fusion. An HCMV-binding domain of 12 aa in the middle hydrophilic region of CMVFR was identified by fusion blocking studies using synthetic receptor peptides. The 1368 bp cDNA of CMVFR contained a predicted ORF of 345 aa with two potential membrane-spanning domains and several possible nuclear localization signals. A search of sequence databases indicated that CMVFR is a novel protein. Further characterization of this cell membrane protein that confers susceptibility to fusion with the viral envelope should provide important information about the mechanism by which HCMV infects cells.
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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, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein H, Cytomegalovirus,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein H, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27-35
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10640539-Amino Acid Sequence,
pubmed-meshheading:10640539-Antibodies, Monoclonal,
pubmed-meshheading:10640539-Base Sequence,
pubmed-meshheading:10640539-Cloning, Molecular,
pubmed-meshheading:10640539-Cytomegalovirus,
pubmed-meshheading:10640539-DNA, Complementary,
pubmed-meshheading:10640539-Epitope Mapping,
pubmed-meshheading:10640539-Humans,
pubmed-meshheading:10640539-Membrane Fusion,
pubmed-meshheading:10640539-Molecular Sequence Data,
pubmed-meshheading:10640539-Receptors, Virus,
pubmed-meshheading:10640539-Sequence Analysis, DNA,
pubmed-meshheading:10640539-Transfection,
pubmed-meshheading:10640539-Tumor Cells, Cultured,
pubmed-meshheading:10640539-Viral Envelope Proteins,
pubmed-meshheading:10640539-Viral Plaque Assay
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pubmed:year |
2000
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pubmed:articleTitle |
Cloning and epitope mapping of a functional partial fusion receptor for human cytomegalovirus gH.
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pubmed:affiliation |
Molecular and Cell Biology Program, University of Maryland School of Medicine, Baltimore, MD 21201, USA. bbald001@umaryland.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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