Comparison of inoculation regimes for the experimental production of swine erysipelas arthritis: II Serological findings in a gel diffusion precipitin test and enzyme-linked immunosorbent assay

The serological response of pigs to Erysipelothrix rhusiopathiae inoculation was monitored by a gel diffusion precipitin test (GDPT) using a crude, serotype-specific, autoclaved antigen and an enzyme-linked immunosorbent assay (ELISA) using a heat-extracted, alcohol precipitated and molecular seived antigen previously shown to react with serum from pigs infected with serotypes 1 or 2. All pigs receiving 3 or 5 weekly intravenous inoculations of either a highly virulent (VRS 229) or a lowly virulent isolate (VRS 252) produced GDPT-reactive antibody within 3 weeks, but only 44% were still reactive at 8 to 9.5 weeks. The ELISA response was significantly higher in pigs inoculated with the highly virulent strain, and was similar in pigs receiving 3 or 5 doses of either strain. In a dose-response trial, after 3 doses of VRS 229, GDPT reactivity occurred earlier and was stronger in pigs given higher doses of E. rhusiopathiae, but the response peaked 3 to 5 weeks after the start of challenge and was short lived. GDPT reactivity correlated with dose, but not with the severity of arthritis. The ELISA demonstrated specific IgG antibody was present by 2 weeks, and persisted to at least 11 weeks. The ELISA reactivity was significantly higher in pigs with arthritis than in pigs that received low doses and were not arthritic. Within groups of pigs with arthritis a significant, dose dependent, linear ELISA response developed but did not correlate with the presence or degree of arthritis at slaughter. Non-arthritic pigs had similar low ELISA responses to uninoculated controls.     

Acetyl-CoA Carboxylase—a Graminicide Target Site

Acetyl-CoA carboxylase catalyses the first committed step in fatty acid (and acyl lipid) formation. The enzyme has been shown to exert a high degree of flux control for lipid biosynthesis in leaves and, therefore, it is not surprising that chemicals which can inhibit it effectively are successful herbicides. These chemicals belong mainly to the cyclohexanedione and aryloxyphenoxypropionate classes and are graminicides. The reason for the selectivity of these herbicides towards grasses lies in the nature of the target site, acetyl-CoA carboxylase. Recent advances in our knowledge of acetyl-CoA carboxylases from sensitive and resistant plants has revealed some important facts. Dicotyledons, which are resistant, have a multi-enzyme complex type of carboxylase in their chloroplasts while grasses have a multifunctional protein. Both divisions of plants have two isoforms of the enzyme, the second being in the cytosol. Detailed study of multifunctional forms of acetyl-CoA carboxylases, which have different sensitivities to herbicides, suggests that herbicide resistance is correlated with cooperativity of herbicide binding to the native dimeric form of the carboxylase. © 1997 SCI.     

Repair scars preserve decadal‐scale patterns of predation intensity despite short‐term ecological disturbances

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