Linked Life Data

6330979

Source:http://linkedlifedata.com/resource/pubmed/id/6330979

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-8-20
pubmed:abstractText
The specificity of neutralizing antibodies for human cytomegalovirus (CMV) envelope proteins was studied by comparing the reactivity of human CMV immune sera with that of a group of CMV-specific monoclonal antibodies. Characterization of this group of monoclonal antibodies revealed that six antibodies bound intact virions, and four of these antibodies neutralized infectious virus in vitro. All of the monoclonal antibodies, as well as human immune sera, precipitated three virion glycoproteins of estimated molecular weights of 160-K 116K, and 55K. Human immune sera also precipitated proteins of estimated molecular weights of 200K, 145K, 100K, 66K, and 34K. The three envelope glycoproteins detected by both the neutralizing monoclonal antibodies and immune human sera were shown to exist as a covalently linked, disulfide-bonded protein complex within virions. This result provided an explanation for the reactivity with multiple proteins of such highly specific reagents as monoclonal antibodies. Furthermore, these findings suggested that determinant(s) detected by CMV-neutralizing antibodies were expressed by this complex of envelope proteins.
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:volume
135
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
369-78
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Neutralizing antibodies detect a disulfide-linked glycoprotein complex within the envelope of human cytomegalovirus.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.