Results 181 to 190 of about 45,419 (204)
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Journal of Microbiology, 2014
VP2 is the minor structural protein of noroviruses (NoV) and may function in NoV particle stability. To determine the function of VP2 in the stability of the NoV particle, we constructed and purified two kinds of virus-like particles (VLPs), namely, VLPs (VP1) and VLPs (VP1+VP2), from Sf9 cells infected with recombinant baculoviruses by using a Bac-to ...
Yao, Lin +4 more
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VP2 is the minor structural protein of noroviruses (NoV) and may function in NoV particle stability. To determine the function of VP2 in the stability of the NoV particle, we constructed and purified two kinds of virus-like particles (VLPs), namely, VLPs (VP1) and VLPs (VP1+VP2), from Sf9 cells infected with recombinant baculoviruses by using a Bac-to ...
Yao, Lin +4 more
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Location of the sequences coding for capsid proteins VP1 and VP2 on polyoma virus DNA
Cell, 1976The 19S and 16S polyoma virus late mRNAs have been separated on sucrose-formamide density gradients and translated in vitro. The 16S RNA codes only for polyoma capsid protein VP1, while the 19S RNA codes in addition for capsid protein VP2. Since the 19S and 16S species have been previously mapped on the viral genome, these results allow us to deduce ...
A E, Smith +4 more
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Expression of VP2 Gene Protein of Infectious Bursal Disease Virus Detected in Korea
Virus Genes, 2003The VP2 gene DNA (1.4 kb in approximate) of a very virulent infectious bursal disease virus (vvIBDV) Chinju strain detected in Chinju, Korea was cloned into the bacmid, a baculovirus shuttle vector, through transposition of the gene from initially cloned pFastBacHTa plasmid, a baculovirus expression vector, and was subsequently expressed in Spodoptera ...
Toh-Kyung, Kim, Sang-Geon, Yeo
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Gene, 1987
A series of expression plasmids was constructed to compare the usefulness of various promoters for the synthesis of a given protein in the Saccharomyces cerevisiae. The plasmids pMBL212, -213, -214, -215 and -216 can be used to synthesize the protein of interest directly as a non-fused protein or, if the protein is difficult to detect, indirectly as an
J M, Verbakel +4 more
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A series of expression plasmids was constructed to compare the usefulness of various promoters for the synthesis of a given protein in the Saccharomyces cerevisiae. The plasmids pMBL212, -213, -214, -215 and -216 can be used to synthesize the protein of interest directly as a non-fused protein or, if the protein is difficult to detect, indirectly as an
J M, Verbakel +4 more
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Virology, 1993
We have used a serotype-specific monoclonal antibody to locate a neutralization epitope on the outer capsid protein, VP2, of the bluetongue virus 13. This surface-accessible region of the virion was recognized by a monoclonal antibody, D24.15, which exhibited serotype-specific neutralizing activity as determined by plaque reduction assay.
G Y, Hwang, J K, Li
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We have used a serotype-specific monoclonal antibody to locate a neutralization epitope on the outer capsid protein, VP2, of the bluetongue virus 13. This surface-accessible region of the virion was recognized by a monoclonal antibody, D24.15, which exhibited serotype-specific neutralizing activity as determined by plaque reduction assay.
G Y, Hwang, J K, Li
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Archives of Virology, 2017
Foot-and-mouth disease (FMD), caused by foot-and-mouth disease virus (FMDV), is a highly contagious infectious disease that affects domestic and wild cloven-hoofed animals worldwide. VP2 is a structural protein of FMDV. In this study, a potent FMDV serotype-independent monoclonal antibody (MAb) 3D9 was generated.
Wenming, Liu +8 more
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Foot-and-mouth disease (FMD), caused by foot-and-mouth disease virus (FMDV), is a highly contagious infectious disease that affects domestic and wild cloven-hoofed animals worldwide. VP2 is a structural protein of FMDV. In this study, a potent FMDV serotype-independent monoclonal antibody (MAb) 3D9 was generated.
Wenming, Liu +8 more
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Epitope mapping of capsid proteins VP2 and VP3 of infectious bursal disease virus
Archives of Virology, 1996Twenty hybridoma cell lines producing monoclonal antibodies (MAbs) against serotype 1 infectious bursal disease virus (IBDV) of GBF-1 and the attenuated GBF-1E strains were produced. The MAbs recognized major structural proteins VP2 and VP3. MAb recognition sites were mapped using recombinant Escherichia coli clones which expressed N-terminal and (or ...
T, Yamaguchi +5 more
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Analysis of DNA-Binding Activity of the JC Virus Minor Capsid Protein VP2
Journal of Neurovirology, 2003To investigate the DNA binding activity of the JC virus minor capsid protein, VP2, both wild-type and mutant VP2 were cloned and expressed in Escherichia coli. Southwestern blotting was employed for the DNA-binding assay. The results showed that VP2 was able to bind to DNA, except when either the last 13 or the last 29 amino acids were truncated.
Yih-Leh, Huang +5 more
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The major antigenic protein of infectious bursal disease virus, VP2, is an apoptotic inducer
Journal of Virology, 1997Infectious bursal disease virus (IBDV) is the causative agent of an economically important poultry disease. Vaccinia virus recombinants expressing the IBDV mature structural capsid proteins VP2 and VP3 were generated by using vectors for inducible gene expression.
A, Fernández-Arias +2 more
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[The surface display of porcine parvovirus VP2 protein in Lactobacillus casei].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2010Lactobacillus casei 393 was selected as a bacterial carrier for the expression of Porcine Parvovirus (PPV) protective antigen VP2 protein. The gene encoding PPV VP2 protein was cloned into the Lactobacillus casei surface expression vector pPG, and then the constructed recombinant vector pPG-VP2 was electrotransformed into Lactobacillus casei 393 ...
Yi-Gang, Xu +8 more
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