SUMMARY: An antiserum, raised in rabbits against honey-bee spiroplasma (BC3) fibril protein monomer, mol. wt 55000, excised from SDS—polyacrylamide gels, had precipitating activity against SDS-denatured fibril protein but not against the native protein. This antiserum was used to probe spiroplasma cell proteins separated by SDS—PAGE and blotted on to nitrocellulose filters. Antigens of mol. wt 55000 were identified in 13 different spiroplasmas, including a non-helical strain of , representing five different sero-groups. The antiserum did not react with proteins in any of the spp. or spp. tested. Two-dimensional immunoelectrophoresis revealed variations in the amount of antigen in different isolates from the same sero-group. Peptide mapping by limited proteolysis showed that the fibril protein was highly conserved within a sero-group but that there was some heterogeneity between groups. All fibril proteins yielded common peptides recognised by the antiserum.


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