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

2000 ◽  
Vol 67 (1) ◽  
pp. 104-111 ◽  
Author(s):  
Min-Ying Wang ◽  
Yung-Yan Kuo ◽  
Meng-Shiou Lee ◽  
Shyue-Ru Doong ◽  
Ji-Yi Ho ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Disease Virus ◽  
Self Assembly ◽  
Infectious Bursal Disease Virus ◽  
Metal Ion ◽  
Insect Cells ◽  
Infectious Bursal Disease ◽  
Bursal Disease ◽  
Virus Capsid Protein ◽  
Metal Ion Affinity Chromatography

scholarly journals Autoproteolytic Activity Derived from the Infectious Bursal Disease Virus Capsid Protein

2009 ◽  
Vol 284 (12) ◽  
pp. 8064-8072 ◽  
Author(s):  
Nerea Irigoyen ◽  
Damià Garriga ◽  
Aitor Navarro ◽  
Nuria Verdaguer ◽  
José F. Rodríguez ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Infectious Bursal Disease ◽  
Virus Capsid ◽  
Bursal Disease ◽  
Virus Capsid Protein

scholarly journals Antigenic Properties and Diagnostic Potential of Baculovirus-Expressed Infectious Bursal Disease Virus Proteins VPX and VP3

2000 ◽  
Vol 7 (4) ◽  
pp. 645-651 ◽  
Author(s):  
Jorge L. Martínez-Torrecuadrada ◽  
Beatriz Lázaro ◽  
José F. Rodriguez ◽  
J. Ignacio Casal
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Neutralizing Antibodies ◽  
Insect Cells ◽  
Indirect Elisa ◽  
Infectious Bursal Disease ◽  
Enzyme Linked Immunosorbent Assay ◽  
Diagnostic Potential ◽  
Antigenic Properties ◽  
Bursal Disease

ABSTRACT The routine technique for detecting antibodies specific to infectious bursal disease virus (IBDV) is a serological evaluation by enzyme-linked immunosorbent assay (ELISA) with preparations of whole virions as the antigens. To avoid using complete virus in the standard technique, we have developed two new antigens through the expression of the VPX and VP3 genes in insect cells. VPX and especially VP3 were expressed at high levels in insect cells and simple to purify. The immunogenicity of both proteins was similar to that of the native virus. VPX was able to elicit neutralizing antibodies but VP3 was not. Purified VPX and VP3 were tested in an indirect ELISA with more than 300 chicken sera. There was an excellent correlation between the results of the ELISA using VPX and those of the two commercial kits. VP3 did not perform as well as VPX, and the linear correlation was significantly lower. A comparison with the standard reference technique, seroneutralization, showed that the indirect ELISA was more sensitive. Therefore, VPX-based ELISA is a good alternative to conventional ELISAs that use whole virions.

scholarly journals The Oligomerization Domain of VP3, the Scaffolding Protein of Infectious Bursal Disease Virus, Plays a Critical Role in Capsid Assembly

2003 ◽  
Vol 77 (11) ◽  
pp. 6438-6449 ◽  
Author(s):  
Antonio Maraver ◽  
Ana Oña ◽  
Fernando Abaitua ◽  
Dolores González ◽  
Roberto Clemente ◽  
...  
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Insect Cells ◽  
Critical Role ◽  
Recombinant Baculovirus ◽  
Particle Formation ◽  
Scaffolding Protein ◽  
Infectious Bursal Disease ◽  
Bursal Disease ◽  
Oligomerization Domain

ABSTRACT Infectious bursal disease virus (IBDV) capsids are formed by a single protein layer containing three polypeptides, pVP2, VP2, and VP3. Here, we show that the VP3 protein synthesized in insect cells, either after expression of the complete polyprotein or from a VP3 gene construct, is proteolytically degraded, leading to the accumulation of product lacking the 13 C-terminal residues. This finding led to identification of the VP3 oligomerization domain within a 24-amino-acid stretch near the C-terminal end of the polypeptide, partially overlapping the VP1 binding domain. Inactivation of the VP3 oligomerization domain, by either proteolysis or deletion of the polyprotein gene, abolishes viruslike particle formation. Formation of VP3-VP1 complexes in cells infected with a dual recombinant baculovirus simultaneously expressing the polyprotein and VP1 prevented VP3 proteolysis and led to efficient virus-like particle formation in insect cells.

scholarly journals Different Architectures in the Assembly of Infectious Bursal Disease Virus Capsid Proteins Expressed in Insect Cells

Virology ◽  
2000 ◽  
Vol 278 (2) ◽  
pp. 322-331 ◽  
Author(s):  
Jorge Luis Martinez-Torrecuadrada ◽  
José R. Castón ◽  
Marian Castro ◽  
José L. Carrascosa ◽  
José F. Rodriguez ◽  
...  
Keyword(s):  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Insect Cells ◽  
Capsid Proteins ◽  
Infectious Bursal Disease ◽  
Virus Capsid ◽  
Bursal Disease
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