A group of 1,623 ovine fecal samples recovered from 65 geographically distinct mutton sheep and prime lamb properties across New South Wales, Australia, were screened for the presence of Shiga toxin-producing Escherichia coli (STEC) virulence factors (stx 1 , stx 2 , eaeA, and ehxA). A subset was cultured for STEC isolates containing associated virulence factors (eaeA and/or ehxA), which were isolated from 17 of 20 (85%) and 19 of 20 (95%) tested prime lamb and mutton sheep properties, respectively. STEC isolates containing stx 1 , stx 2 , and ehxA were most commonly isolated (19 of 40 flocks; 47.5%), and this profile was observed for 10 different serotypes. Among 90 STEC isolates studied, the most common serotypes were O91:H Although isolates belonging to serogroup O157 are regarded as the most clinically significant Shiga toxin-producing Escherichia coli (STEC) strains, the number of non-O157 serotypes recovered from episodes of hemorrhagic colitis and hemolyticuremic syndrome (HUS) continues to increase. Currently over 160 serotypes of E. coli have been isolated from human sources (5,6,13,14,25). Ruminants, in particular (6,7,16,24), but also other domestic animals, including pigs, poultry, cats, and dogs (1,6,8), are natural reservoirs of STEC. Although more than 200 different STEC serotypes have been isolated from cattle (reference 13 and references therein), few studies have extensively examined the presence of STEC in sheep. Existing studies have been performed on comparatively small numbers of sheep or have focused intensively on a single flock or only examined the presence of O157 serotypes (3,12,16,17). Kudva et al. (17) investigated the presence of E. coli O157:H7 in a single flock over a 16-month period and described the presence of non-O157 STEC isolates of serotypes O128:NM, O5:NM, O6:H49, O88:NM, and O91:NM, with various combinations of the virulence-associated genes stx 1 , stx 2 , and eaeA. In Australia, one of the largest sheep-producing countries in the world, recent studies focusing primarily on the southeastern parts of Queensland have suggested that the prevalence of stx in fecal cultures ranges from 69 to 88% (12,22).In this study, we investigated the presence of STEC in fecal enrichment broths derived from 65 geographically diverse flocks of slaughter-age sheep (mutton sheep and prime lambs) in New South Wales, Australia, using a multiplex PCR which detects stx 1 , stx 2 , eaeA, and ehxA (11) and vancomycin-cefixime-cefsulodin blood agar (BVCCA) (18). Mutton sheep and prime lambs represent two different genetic lines of meatproducing animal and comprise sheep of different slaughter ages and production systems, parameters which have been reported to influence STEC colonization in ruminant species (26). Our aim was to isolate STEC strains that contained at least one other virulence factor (eaeA and/or ehxA). These STEC isolates were serotyped and examined for the ability to express Shiga toxins using Vero cell cultures. Commercial properties from 29 prime lamb and 36 mutton sheep flocks we...

In mature retroviral particles, the capsid protein (CA) forms a shell encasing the viral replication complex. Human immunodeficiency virus (HIV) CA dimerizes in solution, through its C-terminal domain (CTD), and this interaction is important for capsid assembly. In contrast, other retroviral capsid proteins, including that of Rous sarcoma virus (RSV), do not dimerize with measurable affinity. Here we show, using X-ray crystallography and other biophysical methods, that acidification causes RSV CA to dimerize in a fashion analogous to HIV CA, and that this drives capsid assembly in vitro. A pair of aspartic acid residues, located within the CTD dimer interface, explains why dimerization is linked to proton binding. Our results show that despite overarching structural similarities, the intermolecular forces responsible for forming and stabilizing the retroviral capsid differ markedly across retroviral genera. Our data further suggest that proton binding may regulate RSV capsid assembly, or modulate stability of the assembled capsid.

No abstract

No abstract