Porin (outer membrane protein) preparations extracted from a rough (Rb2) mutant of Salmonella typhimurium proved to be good immunogens in mice and rabbits. The antibody response achieved was measured by using enzyme-linked immunosorbent assay techniques. High titers of both antiporin and antilipopolysaccharide were detected in both species. The rabbit antiserum raised against the porins and the porn preparations themselves had a highly significant protective capacity against intraperitoneal Salmonella infection of mice. Absorption of the rabbit antiporin serum with lipopolysaccharide immunosorbent did not change its protective capacity in a passive immunization experiment, suggesting that the antiporin antibody preparations were the active components.
Type 1 pili from Salmonella typhimurium LT2 were purified and characterized. The pilus filaments were 6 nm in diameter and over 1 microns long. Estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the molecular weight of the pilin was 21,000. The isoelectric point of the filament was 4.1. Hydrophobic amino acids comprised 40.3% of the total amino acids of the pilin, which contained more proline, serine, and lysine than reported for the type 1 pilin of Escherichia coli. Purified pili agglutinated both horse and chicken erythrocytes and yeast cells but not bovine, sheep, or human erythrocytes. Horse erythrocyte agglutination was inhibited at lower concentrations by alpha-methyl-D-mannoside than by yeast mannane and D-fructose. Agglutination was not affected by D-galactose or sucrose. Results of the present study confirm the role of type 1 pili as Salmonella hemagglutinins and show chemical differences between the type 1 pili of S. typhimurium and E. coli.
A crude major outer membrane (porin) preparation, obtained from a rough strain of Salmonella typhimurium earlier shown to be protective both in active and passive immunization of mice against challenge with smooth S. typhimurium, was further purified. Removal of the main impurities, lipopolysaccharide (LPS) and lipoprotein, was accompanied by loss of protective capacity in passive immunization experiments. Reconstitution with rough LPS restored the protective capacity. Protection was, however, concluded not to be due to anti-LPS, because a large fraction of the anti-LPS antibodies could be removed from the protective rabbit antiserum with an LPS immunosorbent without loss of protection.
tetraacetate (EDTA)-treated envelopes (24). (i) Preparation A. Preparation A was a crude porin preparation obtained as described by Nurminen (24). Lysozyme-EDTA-treated envelopes (25) were extracted twice with 2% (wt/vol) Triton X-100 in the presence of 0.01 M MgCl2; 0.1 g (wet weight
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