Linked Life Data

7595373

Source:http://linkedlifedata.com/resource/pubmed/id/7595373

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-12-19
pubmed:abstractText
The organization of epitopes on the minor capsid protein L2 of human papillomavirus (HPV) type 33 has been analysed using three monoclonal antibodies (MAbs) generated against a large fragment of the L2 protein (amino acids 82-259) expressed as a glutathione S-transferase fusion protein. The topology of the L2 epitopes has been investigated with respect to the structure of HPV-33 virus-like particles (VLPs). Two of the MAbs reacted with linear epitopes which were mapped to amino acids 153-160 and 163-170, respectively. These epitopes were accessible in denatured but not in native VLPs consisting of L1 and L2, suggesting an internal location. The third antibody was unable to detect denatured L2 protein but reacted with native VLPs. This is the first demonstration of an apparent conformational epitope of the HPV L2 protein. A model for the putative orientation of L2 in the papillomavirus capsid is deduced from the location of these and other antigenic sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
76 ( Pt 11)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2661-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Conformational and linear epitopes on virus-like particles of human papillomavirus type 33 identified by monoclonal antibodies to the minor capsid protein L2.
pubmed:affiliation
Institut für Medizinische Mikrobiologie, Johannes-Gutenberg-Universität Mainz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't