RABIES IN ARCTIC FOX (VULPES LAGOPUS) AND REINDEER (RANGIFER TARANDUS PLATYRHYNCHUS) DURING AN OUTBREAK ON SVALBARD, NORWAY, 2011-12.

Rabies is an important zoonotic disease with high fatality rates in animals and humans. In the Arctic, the Arctic fox (Vulpes lagopus) is regarded as the principal reservoir, but there is considerable debate about how the disease persists at the low population densities that are typical for this species. We describe an outbreak of rabies among Arctic foxes and Svalbard reindeer (Rangifer tarandus platyrhynchus) during 2011-12 on the remote Arctic archipelago of Svalbard, an area with a very low and relatively stable Arctic fox density.

Goats naturally devoid of PrP are resistant to scrapie.

Prion diseases are progressive and fatal, neurodegenerative disorders described in humans and animals. According to the "protein-only" hypothesis, the normal host-encoded prion protein (PrP) is converted into a pathological and infectious form (PrP) in these diseases. Transgenic knockout models have shown that PrP is a prerequisite for the development of prion disease.

Stress Resilience of Spermatozoa and Blood Mononuclear Cells without Prion Protein.

The cellular prion protein PrP is highly expressed in neurons, but also present in non-neuronal tissues, including the testicles and spermatozoa. Most immune cells and their bone marrow precursors also express PrP. Clearly, this protein operates in highly diverse cellular contexts.

Goats without Prion Protein Display Enhanced Proinflammatory Pulmonary Signaling and Extracellular Matrix Remodeling upon Systemic Lipopolysaccharide Challenge.

A naturally occurring mutation in the gene of Norwegian dairy goats terminates synthesis of the cellular prion protein (PrP), rendering homozygous goats () devoid of the protein. Although PrP has been extensively studied, particularly in the central nervous system, the biological role of PrP remains incompletely understood. Here, we examined whether loss of PrP affects the initial stage of lipopolysaccharide (LPS)-induced acute lung injury (ALI).

Loss of prion protein induces a primed state of type I interferon-responsive genes.

The cellular prion protein (PrPC) has been extensively studied because of its pivotal role in prion diseases; however, its functions remain incompletely understood. A unique line of goats has been identified that carries a nonsense mutation that abolishes synthesis of PrPC. In these animals, the PrP-encoding mRNA is rapidly degraded.

Activation of innate immune genes in caprine blood leukocytes after systemic endotoxin challenge.

Background: Sepsis is a serious health problem associated with a range of infectious diseases in animals and humans. Early events of this syndrome can be mimicked by experimental administration of lipopolysaccharides (LPS). Compared with mice, small ruminants and humans are highly sensitive to LPS, making goats valuable in inflammatory models.

Hematological shift in goat kids naturally devoid of prion protein.

The physiological role of the cellular prion protein (PrP(C)) is incompletely understood. The expression of PrP(C) in hematopoietic stem cells and immune cells suggests a role in the development of these cells, and in PrP(C) knockout animals altered immune cell proliferation and phagocytic function have been observed. Recently, a spontaneous nonsense mutation at codon 32 in the PRNP gene in goats of the Norwegian Dairy breed was discovered, rendering homozygous animals devoid of PrP(C).