Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2000-2-23
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-35
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Cloning and epitope mapping of a functional partial fusion receptor for human cytomegalovirus gH.
pubmed:affiliation
Molecular and Cell Biology Program, University of Maryland School of Medicine, Baltimore, MD 21201, USA. bbald001@umaryland.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.