Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae

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Abstract
The organization of outer membrane [OM] proteins of N. gonorrhoeae was investigated by using 2-dimensional [sodium] dodecyl sulfate-polyacrylamide gel electrophoresis and cross-linking agents. A naturally-occurring protein aggregate, which may be composed of 2 proteins of 50,000 MW, was detected in all strains. Treatment of whole cells with cross-linking agents yielded several additional complexes, suggesting that other proteins are arranged in the outer membrane as near neighbors. The principal OM protein (MW 34,000) cross-linked to itself to form a complex which appeared to be trimeric, to the 28,000 MW OM protein to form a bimolecular complex and to the 28,000 MW OM protein in a 3:1 ratio. The formation of these complexes was independent of colony type, colony opacity, pH during growth and presence of markers for drug resistance or hypersensitivity. [This may be relevant to the pathogenicity of N. gonorrhoeae].