The intestinal and serum humoral immune response of mice to systemically and orally administered antigens in liposomes: I. The response to liposome-entrapped soluble proteins.

The development of oral vaccines is of great importance in veterinary medicine and new adjuvants and carriers are essential to this aim. Liposomes are effective systemic adjuvants but the relatively little data on their potential as oral adjuvants is inconclusive. Liposomes containing ovalbumin (OA) were effective adjuvants when administered intraperitoneally to mice. Feeding mice with OA or keyhole limpet haemocyanin in liposomes in a series of priming and boosting regimes failed to elicit any significant increase in serum or intestinal antibody response compared with feeding the free antigen. Oral tolerance induction to systemic challenge was also unaffected by OA entrapment in liposomes. In vitro liposome stability assays at 37 degrees C demonstrated a substantial resistance to disruption in the presence of acidic stomach contents. However, the addition of bile caused a rapid and profound release of protein marker from the liposomes. The rate and degree of disruption was influenced by the type of phospholipid used. These results suggest that liposomes may be useful as carriers for orally administered compounds but they are ineffective as adjuvants for the non-particulate, naturally weak immunogens used in this study.     

Plasma Progesterone Profile in Ovariectomized Beef Cows after Intra-vaginal Insertion of New, Once-used or Twice-used CIDR

Objective of this study was to show plasma progesterone concentrations in ovariectomized beef cows after treatment with new, once-used and twice-used controlled internal drug-releasing devices (CIDRs). Four ovariectomized beef cows were used for the experiment. Plasma concentrations of progesterone were quantified using a validated ELISA. The CIDR was inserted into vagina of cows by using a standard CIDR applicator and then removed 7 days after insertion. One week later, once-used CIDR was inserted and removed on day 7. Twice-used CIDR was, then inserted at an interval of 7 days. Mean plasma concentrations of progesterone 24 h after new CIDR insertion was 4.0 ± 0.1 ng/ml, which thereafter decreased gradually to 1.4 ± 0.1 ng/ml at day 7. In cows treated with once-used CIDR or twice-used CIDR, mean plasma progesterone concentrations at day 1 were 2.4 ± 0.2 or 1.8 ± 0.2 ng/ml and 1.0 ± 0 or 0.9 ± 0.1 ng/ml at day 7 respectively. The results suggest that once-used CIDR may be still effective to produce luteal phase progesterone concentrations in plasma in non-suckling beef cows.     

New and unusual causes of acute renal failure in dogs and cats.

This article provides a source for easy reference, summarizing in one location newly recognized and unusual causes of acute renal failure (ARF) in dogs and cats. Several of the causes discussed in this article have been described previously. New or unusual causes of ARF in dogs and cats include infectious diseases (leptospirosis,borreliosis, and babesiosis), nephrotoxicants (aminoglycosides,vitamin D, and nonsteroidal anti-inflammatory drugs), and plant material (lilies and raisins/grapes).     

Risk factors associated with extended spectrum beta-lactamase Escherichia coli (CTX-M) on dairy farms in North West England and North Wales

This study investigated the potential spread of CTX-M-14 Escherichia coli from a known ESBL E. coli positive farm and risk factors for the presence of CTX-M E. coli on dairy farms. Between November 2009 and March 2010, 65 farms in North West England and North Wales were visited and animals sampled for E. coli producing CTX-M ESBLs. Seventeen of these were known to have received animals from a known ESBL E. coli positive 'index' farm since 2005 (linked farms). The prevalence of CTX-M E. coli in the population of linked farms was 58.8% (10/17; CI(95%) 32.9-81.6%) and in the randomly selected control population was 35.4% (17/48; CI(95%) 22.2-50.5%). There was no significant (p>0.05) linkage for the detection of any CTX-M E. coli or specifically a CTX-M-14 E. coli to the index farm. Group 1 (CTX-M-15, CTX-M-55, CTX-M-1, CTX-M-32), group 2 (CTX-M-2) and group 9 (CTX-M-14, CTX-M-14B, CTX-M-27) CTX-M E. coli were identified on the study farms. Molecular analysis revealed that three plasmids from linked farms had similar sizes (95kbp), replicon type (IncK) and backbone genes as that from the index farm. Logistic regression analysis revealed that farms that had used a 3rd or 4th generation cephalosporin (ceftiofur, cefoperazone and cefquinome) in livestock in the last 12months were nearly 4times more likely to have ESBL E. coli present (p=0.037; OR=3.93). There was no significant association between presence of CTX-M E. coli and the use of any 1st or 2nd generation cephalosporins. Several other risk factors for the presence of CTX-M E. coli were identified, such as storage of slurry in a pit, operating an open herd policy and infrequent cleaning of calf feeding equipment.     

Summary of workshop findings for porcine adhesion molecule subgroup

Fifty-nine monoclonal antibodies (mAb) were assigned to the adhesion section of the Second International Swine CD Workshop. They were analysed for their reactivity to selected lymphoid cell populations, as well as to non-lymphoid cell lines. Cell lysate ELISAS and Western Blot analyses were also carried out. As a result, thirteen separate cluster groups emerged (p>0.95). Workshop assignments for adhesion molecules were made: wCD29/49 for mAbs UCP1D2 (#133) and FW4-101 (#165), and PNK-I (#194) and MUC76A (#025) could be assigned to wCD18. For one cluster (FQ1D7, #161 and 2F4, #069) the cellular distribution and MW were characteristic for MHC Class II, and another cluster comprising several antibodies which appeared to recognise MHC Class I. Other clusters could not be assigned to cell surface structures known to be linked to cellular adhesion, however, two further antibodies, 335-2 (#112) and FG1F6 (#156), could be added to SWC1, and the new SWC8 was defined by MIL3 (#077) and MUC20A (#029), binding a ligand of 29–32 kDa. Clustering for these two antibodies was confirmed by blocking studies. The cellular distribution is known for MIL3, recognising an epitope present on granulocytes, B cells, and a subset of T cells expressing CD8 at high intensity.