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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-7-13
pubmed:abstractText
The structure of the icosahedral adenovirus capsid is highly conserved among Adenoviridae. In its native form, the hexon is the major capsid protein. The nascent hexon requires the 100 kDa folding protein to fold into its native, trimeric form. The hexon and 100 kDa folding protein were co-expressed in a fowlpox virus (FPV) vector and in the recombinant FPVs (rFPVs) in which the hexon and 100 kDa folding protein genes are cloned head to tail, the native hexon could be detected with indirect immunofluorescence and immunoprecipitation using a native hexon monoclonal antibody. The FPV-@X100 construct, in which the 100kDa folding protein gene follows the hexon gene in a head to tail fashion, elicited the best humoral response in chickens. An attenuated HEV commercial vaccine elicited higher and longer lasting anti-HEV titers than FPV-@X100. Humoral immunity was also compared in turkeys inoculated with rFPVs expressing the hexon alone, the 100 kDa folding protein alone, or expressing both genes in different configurations. No anti-HEV humoral immune response was detected in turkeys inoculated with the rFPVs expressing the hexon alone or the 100 kDa folding protein alone.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0920-8569
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
353-61
pubmed:dateRevised
2004-10-26
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Characterization of a recombinant fowlpox virus expressing the native hexon of hemorrhagic enteritis virus.
pubmed:affiliation
Department of Pathology, Michigan State University, East Lansing, USA.
pubmed:publicationType
Journal Article