Linked Life Data

10581441

Source:http://linkedlifedata.com/resource/pubmed/id/10581441

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-2-4
pubmed:abstractText
A gene encoding a structural protein (VP2) of a local strain (P3009) of infectious bursal disease virus (IBDV) was cloned and expressed using the baculovirus expression system to develop a subunit vaccine against IBDV infection in Taiwan. The expressed rVP2 proteins formed particles of approximately 20-30 nm in diameter. Those particles were partially purified employing sucrose density gradient ultracentrifugation, and the purified particles were recognized by a monoclonal antibody against the VP2 protein of IBDV P3009. To facilitate the purification of the particles, the VP2 protein was engineered to incorporate a metal ion binding site (His)(6 )at its C-terminus. The chimeric rVP2H proteins also formed particles, which could be affinity-purified in one step with immobilized metal ions (Ni(2+)). Particle formation was confirmed by direct observation under the electron microscope. The production level of rVP2H protein was determined to be 20 mg/L in a batch culture of Hi-5 cells by quantifying the concentration of the purified proteins. The chicken protection assay was performed to evaluate the immunogenicity of the rVP2H protein. When susceptible chickens were inoculated with the recombinant rVP2H proteins (40 microg/bird), virus-neutralizing antibodies were induced, thereby conferring a high level of protection against the challenge of a very virulent strain of IBDV. In conclusion, the most significant finding in this work is that both of the expressed rVP2 and rVP2H proteins can form a particulate structure capable of inducing a strong immunological response in a vaccinated chicken.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3592
pubmed:author
pubmed:copyrightInfo
Copyright 2000 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
104-11
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10581441-Animals, pubmed-meshheading:10581441-Antibodies, Viral, pubmed-meshheading:10581441-Base Sequence, pubmed-meshheading:10581441-Birnaviridae Infections, pubmed-meshheading:10581441-Cell Line, pubmed-meshheading:10581441-Chickens, pubmed-meshheading:10581441-Chromatography, Affinity, pubmed-meshheading:10581441-DNA Primers, pubmed-meshheading:10581441-Gene Expression, pubmed-meshheading:10581441-Genes, Viral, pubmed-meshheading:10581441-Infectious bursal disease virus, pubmed-meshheading:10581441-Nucleopolyhedrovirus, pubmed-meshheading:10581441-Poultry Diseases, pubmed-meshheading:10581441-Recombinant Fusion Proteins, pubmed-meshheading:10581441-Spodoptera, pubmed-meshheading:10581441-Vaccines, Synthetic, pubmed-meshheading:10581441-Viral Structural Proteins, pubmed-meshheading:10581441-Viral Vaccines
pubmed:year
2000
pubmed:articleTitle
Self-assembly of the infectious bursal disease virus capsid protein, rVP2, expressed in insect cells and purification of immunogenic chimeric rVP2H particles by immobilized metal-ion affinity chromatography.
pubmed:affiliation
Graduate Institute of Agricultural Biotechnology National Chung Hsing University, Taichung, Taiwan 40227 ROC. mywang@dragon.nchu.edu.tw
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't