Linked Life Data

8389083

Source:http://linkedlifedata.com/resource/pubmed/id/8389083

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-6-25
pubmed:abstractText
A budding event transfers the immature, single-shelled rotavirus particle (SSP) across the RER membrane prior to assembly of mature virions in the ER lumen. Budding is triggered by the interaction of the SSP with a viral receptor glycoprotein (NS28) which is located in the RER membrane. We have expressed the cytoplasmic domain of the NS28 receptor as a glutathione S-transferase fusion protein to generate a soluble polypeptide that in turn can be cleaved to yield a carboxy-terminal receptor domain. The soluble terminal domain (delta 1-85 NS28) has been purified to homogeneity and retains SSP-binding activity when immobilized on a solid matrix. Integral membrane status therefore is not an essential prerequisite for ligand binding. The Kd for the interaction between immobilized delta 1-85 NS28 and purified particles is 4.6 x 10(-11) M, a value indistinguishable from the value obtained for the full-length and membrane-anchored receptor. Cross-linking with the bifunctional reagent dimethylsuberimidate indicates that delta 1-85 NS28 is a tetramer. When delta 1-85 NS28 is added to a monodisperse suspension of purified virus, the particles aggregate, indicating that the receptor is multivalent. The rotavirus intracellular receptor therefore provides a model for the detailed analysis of the early events that trigger the budding of cytoplasmically located particles across cell membranes.
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:volume
194
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
807-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The RER-localized rotavirus intracellular receptor: a truncated purified soluble form is multivalent and binds virus particles.
pubmed:affiliation
Centre for Gene Technology, School of Biological Sciences, University of Auckland, New Zealand.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't