SummaryThe capsids of human parvovirus B19 consist of two structural proteins, the minor‐capsid protein VP1 and the major‐capsid protein VP2. The latter which constitutes for 95% of the capsid are able to form virus‐like particles (VLPs) in yeast without the presence of VP1‐proteins.
T, Lowin +4 more
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Identification of precursors of structural proteins VP1 and VP2 of hepatitis A virus
Journal of Medical Virology, 1992AbstractThe morphogenetic pathway of hepatitis A virus (HAV), classified as a member of the enteroviruses within the Picornaviridae, still remains obscure and seems to differ considerably from that of poliovirus, the most studied representative of this genus.
, Kusov YYu +5 more
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A mutation increasing the size of the polyoma virion proteins, VP2 and VP3
Virology, 1981Abstract The ts 48 mutant of polyoma virus carries a temperature-sensitive mutation ( ts A) which affects the polyoma large T antigen, blocking viral DNA synthesis at the nonpermissive temperature. In addition, there are at least two other changes in the ts 48 genome which affect virus-coded proteins.
W, Eckhart +4 more
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Phylogenetic comparison of the serotype-specific VP2 protein of bluetongue and related orbiviruses
Virus Research, 1995Regions of the VP2 gene from various bluetongue virus serotypes were sequenced and phylogenetic comparisons were performed. The sequences were characteristic for each BTV serotype and isolates of the same serotype could be grouped geographically, mimicking the topotyping characteristics of BTV VP3 gene sequences. PCR amplification and sequence analysis
L I, Pritchard, A R, Gould
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Analysis of the full-length VP2 protein of canine parvoviruses circulating in Hungary
Archives of Virology, 2014In recent years, the number of cases of disease caused by canine parvovirus 2 (CPV-2) in vaccinated dogs has increased. The aim of the present study was to identify CPV-2 strains present in Hungary. Forty-two out of 50 faecal specimens examined were positive, and 25 VP2 sequences were determined and analysed.
Attila, Cságola +3 more
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Immunogenicity analysis based on VP1 and VP2 proteins of bovine enterovirus
VirologyBovine enterovirus (BEV) infection manifests as a spectrum of clinical signs affecting the respiratory, gastrointestinal, and reproductive systems in cattle. Outbreaks of this disease results in large economic losses to the bovine industry worldwide. Currently there are no efficacious vaccines and medicines to prevent BEV infection.
Yuxin, Peng +10 more
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Identification of the structural proteins of VP1 and VP2 of a novel mud crab dicistrovirus
Journal of Virological Methods, 2011Mud crab dicistrovirus (MCDV), a newly identified single-stranded positive RNA virus, is an important pathogen that causes serious economic losses to mud crab aquaculture. In this study, MCDV was purified, and three structural proteins of MCDV were separated by SDS-PAGE.
Rui, Zhang +7 more
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Cell-free synthesis of polyoma virus capsid proteins VP1 and VP2
Journal of Virology, 1977Polyadenylated RNA isolated from the cytoplasm of mouse 3T6 cells 28 h after infection with polyoma virus has been isolated and translated in vitro. Polyoma capsid proteins VP1 and VP2 have been identified in the cell-free product by polyacrylamide gel electrophoresis, specific immunoprecipitation, and tryptic peptide fingerprinting.
T, Wheeler +4 more
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The immunogenicity of the virus-like particles derived from the VP2 protein of porcine parvovirus
Veterinary Microbiology, 2020Porcine parvovirus (PPV) is a major cause of the syndrome of sow reproductive failure that can cause economic losses. In this study, we developed a subunit vaccine against porcine parvovirus (PPV), composed of virus-like particles (VLPs) derived from a prokaryotic system, and evaluated its potential against PPV infection.
Tao, Hua +5 more
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Production and immunogenicity of VP2 protein of porcine parvovirus expressed in Pichia pastoris
Archives of Virology, 2013Viral protein 2 (VP2) of porcine parvovirus (PPV) is the major viral structural protein and is responsible for eliciting neutralizing antibodies in immunized animals. In this study, we constructed and characterized a recombinant yeast vector encoding the VP2 protein, designated as pGAPZαA-VP2. The construct was confirmed by restriction enzyme digestion,
Chunhe, Guo, Zemin, Zhong, Yumao, Huang
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