Response to Antigenic Determinants of Neisseria Meningitidis Lipopolysaccharide Investigated with A New Radioactive Antigen-Binding Assay

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Abstract
Adaptations of the Farr technique have resulted in a specific and reproducible radioactive antigen-binding assay for antibodies directed against the lipopolysaccharide (LPS) of Neisseria meningitidis. LPS was intrinsically labeled with 14C acetate during 16-hr growth in a modified Frantz media, extracted by hot phenol-H2O, and purified by dialysis, ultracentrifugation, and ethanol precipitation. LPS, which aggregates in aqueous solutions, was maintained in a monomeric form in 3% sodium deoxycholate (NaD) as determined by gel filtration on Sephadex G-75. Since NaD is insoluble in (NH4)2SO4, polyethylene glycol, 20%, was used to precipitate immunoglobulins of all three major classes. Data obtained with the assay provide evidence that host responses to meningococcal LPS vary both quantitatively and qualitatively. Preliminary investigations of these differences by ultra high resolution chromatography indicate that the binding of unchromatographed or “native” LPS represents the summation of individual binding of antigenically distinct molecules, and that the response to these individual determinants within a given LPS may vary considerably from one host to another.

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