Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-5-12
pubmed:abstractText
Virus-like particles with genetically defined envelope proteins were generated from cDNA in order to examine the requirement of Sendai virus haemagglutinin-neuraminidase (HN) protein for particle formation, and the role of fusion protein (F) in receptor binding and membrane fusion. Characterization of particles devoid of HN protein showed that particle formation was unimpaired by the absence of HN protein, indicating that HN protein is dispensable for virus assembly and budding. Infection studies further demonstrated that virus adsorption and penetration can be mediated solely by the F protein when the human asialoglycoprotein receptor is present at the surface of host cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
79 ( Pt 4)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
683-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9568961-3T3 Cells, pubmed-meshheading:9568961-Animals, pubmed-meshheading:9568961-Asialoglycoprotein Receptor, pubmed-meshheading:9568961-Base Sequence, pubmed-meshheading:9568961-Chloramphenicol O-Acetyltransferase, pubmed-meshheading:9568961-DNA, Complementary, pubmed-meshheading:9568961-Genes, Reporter, pubmed-meshheading:9568961-Hemagglutinins, Viral, pubmed-meshheading:9568961-Humans, pubmed-meshheading:9568961-Membrane Fusion, pubmed-meshheading:9568961-Mice, pubmed-meshheading:9568961-Microscopy, Electron, pubmed-meshheading:9568961-Neuraminidase, pubmed-meshheading:9568961-Receptors, Cell Surface, pubmed-meshheading:9568961-Respirovirus, pubmed-meshheading:9568961-Viral Fusion Proteins, pubmed-meshheading:9568961-Viral Proteins, pubmed-meshheading:9568961-Virus Replication
pubmed:year
1998
pubmed:articleTitle
Sendai virus-like particles devoid of haemagglutinin-neuraminidase protein infect cells via the human asialoglycoprotein receptor.
pubmed:affiliation
Abteilung für Virusforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't