Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1992-7-13
pubmed:abstractText
Capsids of the B19 parvovirus are composed of major (VP2; 58 kD) and minor (VP1; 83 kD) structural proteins. These proteins are identical except for a unique 226 amino acid region at the amino terminus of VP1. Previous immunization studies with recombinant empty capsids have demonstrated that the presence of VP1 was required to elicit virus-neutralizing antibody activity. However, to date, neutralizing epitopes have been identified only on VP2. Crystallographic studies of a related parvovirus (canine parvovirus) suggested the unique amino-terminal portion of VP1 assumed an internal position within the viral capsid. To determine the position of VP1 in both empty capsids and virions, we expressed a fusion protein containing the unique region of VP1. Antisera raised to this protein recognized recombinant empty capsids containing VP1 and VP2, but not those containing VP2 alone, in an enzyme-linked immunosorbent assay. The antisera immunoprecipitated both recombinant empty capsids and human plasma-derived virions, and agglutinated the latter as shown by immune electron microscopy. The sera contained potent neutralizing activity for virus infectivity in vitro. These data indicate that a portion of the amino terminus of VP1 is located on the virion surface, and that this region contains intrinsic neutralizing determinants. The external location of the VP1-specific tail may provide a site for engineered heterologous epitope presentation in novel recombinant vaccines.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-1647068, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-1701479, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-1705987, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-1711206, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-1716693, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-1719240, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2006420, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2157861, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2173460, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2422392, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2476528, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2479578, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2542797, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2551923, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2837357, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2838911, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-2838958, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-3038211, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-3701931, http://linkedlifedata.com/resource/pubmed/commentcorrection/1376332-3738514
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9738
pubmed:author
pubmed:issnType
Print
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2023-9
pubmed:dateRevised
2010-9-7
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface.
pubmed:affiliation
Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.
pubmed:publicationType
Journal Article