Effect of aluminum ions on chemical and immunological properties of meningococcal group B polysaccharide.
Soluble salts of aluminum were examined for their capacity to complex with purified meningococcal group B polysaccharide. The formation of the complexes resulted, first, in a markedly reduced rate of internal esterification at acid pH and, consequently, prolonged stability of the antigen as measured by its reactivity with antibody at pH 4 and, second, in an increased resistance to neuraminidase. Al3+ complexes of B polysaccharides were tested for immunogenicity in mice and found to be no better than the purified polysaccharide in the Na+ or Ca2+ form. However, when Neisseria meningitidis type 6 protein (outer membrane) complexed to B polysaccharide was tested, a substantial increase in anti-B titers was detected, whereas antiprotein titers remained unchanged. The possibility of using combinations of metal-polysaccharide-outer membrane protein complexes as vaccines for humans is discussed.
D000535:Aluminum / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D003378:Counterimmunoelectrophoresis; D005260:Female; D006863:Hydrogen-Ion Concentration; D007114:Immunization; D007477:Ions; D051379:Mice; D008808:Mice, Inbred CBA; D009345:Neisseria meningitidis / Q000187:drug effects / Q000276:immunology*; D009439:Neuraminidase / Q000494:pharmacology; D011135:Polysaccharides, Bacterial / Q000276:immunology*; D011817:Rabbits; D012794:Sialic Acids / Q000378:metabolism
D007477:Ions; D011135:Polysaccharides, Bacterial; D012794:Sialic Acids; D000535:Aluminum; D009439:Neuraminidase