Transmissible spongiform encephalopathies (TSEs), or prion diseases, are mammalian neurodegenerative disorders characterized by a posttranslational conversion and brain accumulation of an insoluble, protease-resistant isoform (PrP Sc ) of the host-encoded cellular prion protein (PrP C ). Human and animal TSE agents exist as different phenotypes that can be biochemically differentiated on the basis of the molecular mass of the protease-resistant PrP Sc fragments and the degree of glycosylation. Epidemiological, molecular, and transmission studies strongly suggest that the single strain of agent responsible for bovine spongiform encephalopathy (BSE) has infected humans, causing variant Creutzfeldt-Jakob disease. The unprecedented biological properties of the BSE agent, which circumvents the so-called ''species barrier'' between cattle and humans and adapts to different mammalian species, has raised considerable concern for human health. To date, it is unknown whether more than one strain might be responsible for cattle TSE or whether the BSE agent undergoes phenotypic variation after natural transmission. Here we provide evidence of a second cattle TSE. The disorder was pathologically characterized by the presence of PrP-immunopositive amyloid plaques, as opposed to the lack of amyloid deposition in typical BSE cases, and by a different pattern of regional distribution and topology of brain PrP Sc accumulation. In addition, Western blot analysis showed a PrP Sc type with predominance of the low molecular mass glycoform and a protease-resistant fragment of lower molecular mass than BSE-PrP Sc . Strikingly, the molecular signature of this previously undescribed bovine PrP Sc was similar to that encountered in a distinct subtype of sporadic Creutzfeldt-Jakob disease.

Deformed wing virus (DWV) of honeybees (Apis mellifera) is closely associated with characteristic wing deformities, abdominal bloating, paralysis, and rapid mortality of emerging adult bees. The virus was purified from diseased insects, and its genome was cloned and sequenced. The genomic RNA of DWV is 10,140 nucleotides in length and contains a single large open reading frame encoding a 328-kDa polyprotein. The coding sequence is flanked by a 1,144-nucleotide 5 nontranslated leader sequence and a 317-nucleotide 3 nontranslated region, followed by a poly(A) tail. The three major structural proteins, VP1 (44 kDa), VP2 (32 kDa), and VP3 (28 kDa), were identified, and their genes were mapped to the N-terminal section of the polyprotein. The C-terminal part of the polyprotein contains sequence motifs typical of well-characterized picornavirus nonstructural proteins: an RNA helicase, a chymotrypsin-like 3C protease, and an RNA-dependent RNA polymerase. The genome organization, capsid morphology, and sequence comparison data indicate that DWV is a member of the recently established genus Iflavirus.Deformed wing virus (DWV) is the one of the main viruses associated with the collapse of honeybee (Apis mellifera L.) colonies due to infestation with the ectoparasitic mite Varroa destructor (4,8,12). The virus was first isolated from a sample of symptomatic honeybees from Japan in the early 1980s and is currently distributed worldwide, wherever varroa mites are found (2, 18). A recent survey of adult bee populations detected DWV in over 90% of French apiaries (66) and in 100% of mite samples. The incidence was slightly reduced when pupal samples were analyzed, especially in the spring (66). DWV has also been detected by serology in the dwarf bee A. florae Fabr. (F. R. Hunter-Fujita, M. S. Mossadegh, and B. V. Ball, Abstr. 36th "Apimondia" Int. Apic. Congr., abstr. 230, 1999) and in the Asian honeybee A. cerana Fabr. (2) and by reverse transcriptase (RT) PCR in bumblebees (29). It is serologically related to Egypt bee virus (8, 9, 13), first isolated in 1977 from infected adults from Egypt (10). Typical symptoms of deformed wing disease are vestigial and crumpled wings, bloated abdomens, paralysis, and a severely shortened adult life span for emerging worker and drone bees (44). For a long time it was believed that these symptoms were due to the feeding activity of the mites (23, 42, 72) until it was shown that, in diseased colonies, deformed bees could emerge from cells not parasitized by varroa mites (49, 55) and that the symptoms can persist in the absence of mites (13). The symptoms are perfectly correlated with the presence of large amounts of DWV, as well as with the reduced virus titers and lower prevalence found in asymptomatic bees from the same colonies (17,19,20,54,67,68). The combination of mites and virus causes immunosuppression in the bees and increased susceptibility to other opportunistic pathogens (76), leading to a progressive reduction in colony performance and a complex disease profile at colony level...

Since summer 2010, numerous cases of Rabbit Haemorrhagic Disease (RHD) have been reported in north-western France both in rabbitries, affecting RHD-vaccinated rabbits, and in wild populations. We demonstrate that the aetiological agent was a lagovirus phylogenetically distinct from other lagoviruses and which presents a unique antigenic profile. Experimental results show that the disease differs from RHD in terms of disease duration, mortality rates, higher occurrence of subacute/chronic forms and that partial cross-protection occurs between RHDV and the new RHDV variant, designated RHDV2. These data support the hypothesis that RHDV2 is a new member of the Lagovirus genus. A molecular epidemiology study detected RHDV2 in France a few months before the first recorded cases and revealed that one year after its discovery it had spread throughout the country and had almost replaced RHDV strains. RHDV2 was detected in continental Italy in June 2011, then four months later in Sardinia.

Neutralizing monoclonal antibodies (nMAbs) elicited against foot-and-mouth disease virus (FMDV) of serotype C were assayed with field isolates and variant FMDVs using several immunoassays. Of a total of 36 nMAbs tested, 23 recognized capsid protein VP1 and distinguished at least 13 virion conformationindependent epitopes involved in neutralization of FMDV C. Eleven epitopes of FMDV C-S8cl have been located in segments 138-156 or 192-209 of VP1 by quantifying the reactivity of nMAbs with synthetic peptides and with nMAb-resistant mutants of FMDV C-S8cl carrying defined amino acid substitutions. The main antigenic site of FMDV C-S8cl (VP1 residues 138 to 150) consists of multiple (at least 10), distinguishable, overlapping epitopes. Some amino acid replacements abolished one of the epitopes, whereas other replacements affected several epitopes in this region. The conservative substitution His(146) --, Arg, found in many nMAb-resistant mutants analysed, abolished the reactivity of the virus with all nMAbs that recognized epitopes in the main antigenic site of FMDV C-S8cl. This indicates that a minimum genetic change can result in a highly amplified phenotypic effect, as regards the antigenicity of FMDV.