Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1998-8-3
pubmed:abstractText
Five overlapping segments of the VP60 capsid protein gene of rabbit haemorrhagic disease virus have been expressed in E. coli under the control of the T7 RNA polymerase. After purification, the antigenicity of these denatured protein segments has been studied by reactivity with sera from both naturally infected and vaccinated animals in Western blot analysis. The amino terminus segments of the protein (comprising the first 175 amino acids) are highly reactive with the tested sera, between 10 and 100 fold more than any of the segments reproducing the carboxy half of VP60, which is believed to be solvent-exposed in the virus particles. These results strongly suggest that the antigenic structure of the carboxy moiety of VP60 is mainly based on conformation-dependent B-cell epitopes whereas the amino terminal region of VP60 contains continuous antigenic determinants for the immune response elicited during both virus infection and exposure to the inactivated vaccine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0304-8608
pubmed:author
pubmed:issnType
Print
pubmed:volume
142
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1843-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Antigenicity of VP60 structural protein of rabbit haemorrhagic disease virus.
pubmed:affiliation
Institut de Biologia Fonamental, Universitat Autònoma de Barcelona, Bellaterra, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't