Recombinant baculoviruses were used to produce human B19 parvovirus empty capsids composed of only VP2 and VP2 capsids containing 4%, 25%, 35%, or 41% VP1 protein. Immunogenicity of the purified capsids, formulated with or without adjuvant, was evaluated in mice, guinea pigs, and rabbits. Sera were analyzed for total anti-B19 parvovirus antibodies, antibodies specific to the region unique to the VP1 capsid protein, and virus neutralizing antibodies. A relationship was observed between the development of antibodies specific to sequences unique to the VP1 protein and virus neutralization. The polypeptide composition of the empty capsid immunogens appeared to be important for elicitation of potent virus neutralizing activity. VP2 capsid immunogens devoid of VP1 protein, or consisting of only 4% VP1, the composition of naturally occurring virions, were generally poor at eliciting high levels of virus neutralizing activity. Capsids consisting of > or = 25% VP1 protein efficiently and consistently provoked vigorous B19 virus neutralizing responses. Recombinant empty capsids enriched for the VP1 protein should serve as the basis for a human B19 parvovirus vaccine.
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http://dx.doi.org/10.1093/infdis/167.5.1034 | DOI Listing |
PLoS Pathog
January 2025
State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Foot-and-mouth disease virus (FMDV) are small, icosahedral viruses that cause serious clinical symptoms in livestock. The FMDV VP1 protein is a key structural component, facilitating virus entry. Here, we find that the E3 ligase RNF5 interacts with VP1 and targets it for degradation through ubiquitination at the lys200 of VP1, ultimately inhibiting virus replication.
View Article and Find Full Text PDFGene
January 2025
National Institute of Animal Biotechnology, Hyderabad, Telangana 500032, India; Regional Center for Biotechnology (RCB), Faridabad, Haryana, India. Electronic address:
Duck viral hepatitis (DVH) caused by duck hepatitis A virus (DHAV) is a highly contagious and economically important disease of ducklings worldwide. In many parts of the globe, disease outbreaks are reported in spite of vaccinations, probably due to antigenic diversity among DHAV genotypes. We previously reported the first isolation of DHAV-2 (Genotype-2) from ducklings in Tamil Nadu, India.
View Article and Find Full Text PDFHeliyon
March 2024
Department of Microbiology, University of Dhaka, Dhaka, 1000, Bangladesh.
Foot-and-mouth disease virus (FMDV), the causative agent of the foot-and-mouth disease of cattle population possesses a rapid evolutionary rate. In Bangladesh, the first circulation of the O/ME-SA/SA-2018 lineage as a novel sublineage, MYMBD21 was reported from our laboratory. The first whole genome sequence of an isolate, BAN/MY/My-466/2021 (shortly named My-466) of the SA-2018 lineage is characterized and represented in this study.
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December 2024
Xinjiang Key Laboratory of New Drug Study and Creation for Herbivorous Animals (XJ-KLNDSCHA), College of Veterinary Medicine, Xinjiang Agricultural University, Urumqi 830052, China.
Porcine bocavirus (PBoV), classified within the genus Bocaparvovirus, has been reported worldwide. PBoV has been divided into group 1, group 2, and group 3. PBoV group 3 (G3) viruses are the most prevalent in China.
View Article and Find Full Text PDFViruses
November 2024
MRC-University of Glasgow Centre for Virus Research, Garscube Campus, 464 Bearsden Road, Glasgow G61 1QH, UK.
Caliciviruses are a diverse group of non-enveloped, positive-sense RNA viruses with a wide range of hosts and transmission routes. Norovirus is the most well-known member of the ; the acute gastroenteritis caused by human norovirus (HuNoV), for example, frequently results in closures of hospital wards and schools during the winter months. One area of calicivirus biology that has gained increasing attention over the past decade is the conformational flexibility exhibited by the protruding (P) domains of the major capsid protein VP1.
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