1985 Volume 31 Issue 4 Pages 347-357
Immunological cross-reactivities among intracellular proteins, sulfite reductase and hydrogenase, and somatic antigens of Desulfovibrio strains were investigated. Antisera were prepared against purified sulfite reductases of Desulfovibrio vulgaris, strain Miyazaki K (MK), and strain Miyazaki F (MF). In double diffusion test, these two antisera (γ-globulin fractions) gave a single fused precipitin line or sometimes with a spur, or crossing. These variants occurred with crude extracts from D. vulagaris, strains MK, MF, Miyazaki Y (MY), and HildenboroughT (subsp. vulgaris), D. desulfuricans subsp. desulfuricans, strains Essex 6T, NRC 49001, and Norway 4, D. gigas NCIB 9332T, D. africanus BenghaziT, and D. salexigens British GuianaT, as well as with the purified enzymes from MK and MF. The relationship among these sulfite reductases is discussed considering the pattern of spur formation. Sulfite reductase activity in crude extracts from these strains was decreased by adding the two antisera, though the levels of decrease varied with strains. Antiserum against hydrogenase from MK cross-reacted with hydrogenases from strains Hildenborough and NRC 49001 but not with those from the other strains. Agglutination tests with antisera prepared against somatic antigens of the three strains, MK, Hildenborough, and MF, revealed that cross-reaction among strains was rather restricted. The three strains, MK, Hildenborough, and NRC 49001, shared common somatic antigens and the two strains, MF and MY, had others in common, but the cells of the other strains were not agglutinated with these antisera.