Subject(s)
Gadiformes/immunology , Immunoglobulins/chemistry , Immunoglobulins/metabolism , Animals , Chromatography, Gel/veterinary , Immunoglobulins/blood , Immunoglobulins/isolation & purification , Molecular Weight , Protein Isoforms/isolation & purification , Protein Structure, Quaternary , Salmo salar/immunology , Species SpecificityABSTRACT
A family of outer membrane lipoproteins of Neisseria meningitidis, LP2086, has been shown to induce serum bactericidal activity against a broad variety of meningococcal strains. Two sub-families of serologically distinct LP2086 proteins (A and B) have been identified. In the present study, we have shown that polyclonal anti-serum against rLP2086 is protective in vivo in an infant rat passive-protection model. Additionally, the LP2086 protein is displayed on the surface of 91% meningococcal strains as measured in a whole cell ELISA using polyclonal anti-sera raised against these proteins. We also demonstrate based on the reactivity of anti-rLP2086 antibody with recombinantly expressed C- and N-terminal fragments of rLP2086 in a Western blot assay that the C-terminal fragment of LP2086 dictates sub-family specificity and the N-terminal fragment determines the family specificity. A formulation containing family A and B of LP2086 potentially would provide broad protection against a majority of Neisseria meningitidis strains.
