Oral immunization of wild boar and domestic pigs with attenuated live vaccine protects against Pseudorabies virus infection.

In domestic pigs strict control measures and the use of gene-deleted marker vaccines resulted in the elimination of pseudorabies virus (PrV) infections in many parts of Europe and North America. In free-roaming feral pigs and wild boar populations, however, serological surveys and monitoring in The Americas, Europe and North Africa provided serological and virological evidence that PrV is more widely distributed than previously assumed. Thus, there is a constant risk of spillover of PrV infection from wild pig populations to domestic animals which could require intervention to limit the infection in wild pigs.

Ultrastructural analysis of virion formation and intraaxonal transport of herpes simplex virus type 1 in primary rat neurons.

After primary replication at the site of entry into the host, alphaherpesviruses infect and establish latency in neurons. To this end, they are transported within axons retrograde from the periphery to the cell body for replication and in an anterograde direction to synapses for infection of higher-order neurons or back to the periphery. Retrograde transport of incoming nucleocapsids is well documented.

Novel hepatitis E virus genotype in Norway rats, Germany.

Human hepatitis E virus infections may be caused by zoonotic transmission of virus genotypes 3 and 4. To determine whether rodents are a reservoir, we analyzed the complete nucleotide sequence of a hepatitis E-like virus from 2 Norway rats in Germany. The sequence suggests a separate genotype for this hepatotropic virus.

Ultrastructural analysis of virion formation and anterograde intraaxonal transport of the alphaherpesvirus pseudorabies virus in primary neurons.

A hallmark of alphaherpesviruses is their capacity to be neuroinvasive and establish latent infections in neurons. After primary replication in epithelial cells at the periphery, entry into nerve endings occurs, followed by retrograde transport of nucleocapsids to the nucleus where viral transcription, genome replication, and nucleocapsid formation take place. Translocation of nucleocapsids to the cytoplasm is followed by axonal transport to infect synaptically linked neurons.

In vitro and in vivo characterization of glycoprotein C-deleted infectious laryngotracheitis virus.

Infectious laryngotracheitis is an important respiratory disease of chickens that is caused by an alphaherpesvirus [infectious laryngotracheitis virus (ILTV); Gallid herpesvirus 1]. As herpesvirus envelope glycoproteins are main targets of the humoral host immune response, they are of particular interest for development of vaccines, as well as of diagnostic tools. The conserved, N-glycosylated envelope protein gC has been identified as a major surface antigen of ILTV.

Pathogenesis and transmission of the novel swine-origin influenza virus A/H1N1 after experimental infection of pigs.

Influenza virus A/H1N1, which is currently causing a pandemic, contains gene segments with ancestors in the North American and Eurasian swine lineages. To get insights into virus replication dynamics, clinical symptoms and virus transmission in pigs, we infected animals intranasally with influenza virus A/Regensburg/D6/09/H1N1. Virus excretion in the inoculated pigs was detected in nasal swabs from 1 day post-infection (p.

Deletion or green fluorescent protein tagging of the pUL35 capsid component of pseudorabies virus impairs virus replication in cell culture and neuroinvasion in mice.

To facilitate tracing of virion movement, the non-essential capsid proteins pUL35 of herpes simplex virus type 1 and pseudorabies virus (PrV) have been tagged with green fluorescent protein (GFP). However, the biological relevance of PrV pUL35 and the functionality of the fusion proteins have not yet been investigated in detail. We generated PrV mutants either lacking the 12 kDa UL35 gene product, or expressing GFP fused to the N terminus of pUL35.

Mutagenesis of the active-site cysteine in the ubiquitin-specific protease contained in large tegument protein pUL36 of pseudorabies virus impairs viral replication in vitro and neuroinvasion in vivo.

Herpesviruses specify a ubiquitin-specific protease activity located within their largest tegument protein. Although its biological role is still largely unclear, mutation within the active site abolished deubiquitinating (DUB) activity and decreased virus replication in vitro and in vivo. To further elucidate the role of DUB activity for herpesvirus replication, the conserved active-site cysteine at amino acid position 26 within pUL36 of Pseudorabies virus (PrV) (Suid herpesvirus 1), a neurotropic alphaherpesvirus, was mutated to serine.

Residual infectious disease risk in screened blood transfusion from a high-prevalence population: Santa Catarina, Brazil.

Background: Infectious disease testing has improved but viral infection transmission through transfusion continues to occur. Residual risk, however, is now so low in some countries that it can only be estimated by mathematical modeling. With hierarchical Bayesian methods, this study estimates the residual risk of transfusion-transmitted infections in Santa Catarina, Brazil.

Identification of functional domains within the essential large tegument protein pUL36 of pseudorabies virus.

Proteins of the capsid proximal tegument are involved in the transport of incoming capsids to the nucleus and secondary envelopment after nuclear egress. Homologs of the essential large capsid proximal tegument protein pUL36 are conserved within the Herpesviridae. They interact with another tegument component, pUL37, and contain a deubiquitinating activity in their N termini which, however, is not essential for virus replication.

Relevance of the interaction between alphaherpesvirus UL3.5 and UL48 proteins for virion maturation and neuroinvasion.

The UL3.5 and UL48 genes, which are conserved in most alphaherpesvirus genomes, are important for maturation of pseudorabies virus (PrV) particles in the cytoplasm of infected cells (W. Fuchs, B.