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The A1, A2, B1, and B2 species of bovine alpha crystallin have been purified and renatured to form high molecular weight aggregates comprised of only one species, and the aggregated forms of each of these species have been tested for their ability to bind to lens membrane in vitro. The aggregated forms of alpha-A1 and alpha-A2 bound to membrane in a saturable manner while those of alpha-B1 and alpha-B2 bound in much lower amounts, in a manner inconsistent with saturable binding. Together, these results demonstrate specific and saturable binding of aggregated alpha-A1 and alpha-A2 to the lens membrane, suggesting that these species are responsible for the previously observed interaction between alpha crystallin and the lens fiber cell membrane.

Antiserum to a partially purified neuraminidase from Pasteurella multocida, type A:3, was adsorbed with protease-digested P. multocida type 3 lipopolysaccharide (LPS) to remove LPS immunoreactivity. The LPS-adsorbed antineuraminidase caused a 77% reduction in the neuraminidase activity of homologous P. multocida in an in vitro enzyme neutralization test. All 14 mice passively immunized with the adsorbed antineuraminidase were protected against challenge infection with homologous P. multocida in a mouse protection test. Ten out of 14 mice in one group that received antisera containing antibodies to both neuraminidase and LPS were protected. In contrast, only 1 out of 14 mice that were immunized with pre-immune serum survived the challenge. These results suggest that antiserum to P. multocida neuraminidase was, at least partly, responsible for the protection observed in this study. Neuraminidase may be one of the immunogenic protective proteins present in aqueous extracts of Pasteurella multocida.

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