Subject(s)
Abruptio Placentae/etiology , Uterine Diseases/complications , Abruptio Placentae/diagnosis , Abruptio Placentae/surgery , Adult , Female , Humans , Pregnancy , Torsion Abnormality/complications , Torsion Abnormality/diagnosis , Torsion Abnormality/surgery , Uterine Diseases/diagnosis , Uterine Diseases/surgeryABSTRACT
A recombinant baculovirus (Bac-EgB) containing the complete open reading frame of equine herpesvirus 1 glycoprotein B (EHV-1 gB) expressed recombinant products of 107-133 kDa, 58-75 kDa and 53-57 kDa, corresponding to EHV-1 gB precursor, large and small subunits respectively. High molecular mass products (>200 kDa) in the Bac-EgB infected insect cells were consistent with oligomerisation of the recombinant EHV-1 gB products, and analysis with tunicamycin and endoglycosidases indicated that the baculovirus-expressed gB contained N-linked sugars with high mannose and hybrid chains. N-terminal amino acid sequence analysis of the gB forms revealed identical signal and endoproteolytic cleavage sites to those of gB in EHV-1 infected mammalian cells, and authenticity of processing and transport was supported by the presence of EHV-1 gB antigen at the surface of infected insect cells. Immunogold labelling and electron microscopy of recombinant baculovirus particles indicated that the recombinant gB was also present in baculovirus envelopes. Bac-EgB infected insect cells were able to induce low levels of complement dependent virus neutralising antibody, and have been shown to evoke protective immune responses in murine models of respiratory disease and abortion.
Subject(s)
Glycoproteins/chemistry , Herpesviridae Infections/veterinary , Herpesvirus 1, Equid/genetics , Horse Diseases/virology , Viral Envelope Proteins/chemistry , Animals , Antibodies, Monoclonal , Baculoviridae/genetics , DNA Primers/chemistry , DNA, Viral/chemistry , Electrophoresis, Polyacrylamide Gel/veterinary , Gene Expression Regulation, Viral , Glycoproteins/genetics , Glycoside Hydrolases/chemistry , Herpesviridae Infections/virology , Horses , Microscopy, Fluorescence/veterinary , Microscopy, Immunoelectron/veterinary , Molecular Weight , Open Reading Frames , Polymerase Chain Reaction/veterinary , Recombinant Proteins/chemistry , Tunicamycin/chemistry , Viral Envelope Proteins/geneticsABSTRACT
The experiments reported here investigate the conditionability, using taste aversion conditioning, of the antagonistic effects of alpha-MSH on the thermoregulatory changes associated with injection of bacterial endotoxin lipopolysaccharide (LPS) in rats. Animals were administered LPS and then given alpha-MSH, as an unconditioned stimulus (UCS), in association with the novel taste of saccharin, the conditioned stimulus (CS). The temperature response at this time in alpha-MSH-treated rats was similar to that observed in control animals. However, 7 days later, when these animals were again injected with LPS but re-exposed to saccharin alone, there was a significant reduction in the temperature response profile compared to controls. These results demonstrate that in male rats the conditioned antipyretic effect following conditioning with alpha-MSH as the UCS is sufficiently robust to counteract the acute effects on body temperature of an LPS injection at the time of CS reexposure. This complements previous experiments demonstrating that thermoregulation may be influenced by cognitive association.
