CHARACTERIZATION OF DETERGENT-SOLUBLE PROTEINS OF CORYNEBACTERIUM-PSEUDOTUBERCULOSIS

Whole cells and culture supernatant of isolates of Corynebacterium pse udotuberculosis were studied by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting (immunoblotting). SDS-PAGE analysis of detergent-solublized whole cells revealed more t han 20 bands in silver-stained gels. However, the SDS-soluble proteins that are present in all the isolates of the bacterium can be separate d into four groups, as follows, (i) high molecular mass proteins that are greater than 119 kDa, (ii) a set of three proteins with molecular mass of 84, 64 and 58 kDa, (iii) a doublet consisting of proteins of m olecular mass 33 to 30 kDa, and (iv) low molecular mass proteins of 25 to 20 kDa. SDS-PAGE analysis of ammonium sulphate concentrated cultur e supernatant demonstrated more than seven bands in silver-stained gel s ranging in molecular mass from 64-14 kDa. Sera from goats with C.pse udotuberculosis-induced disease were used to probe immunoblots of elec trophoresed SDS-soluble proteins. Ten or more SDS-soluble proteins fro m whole cells, ranging in molecular mass from 119-20 kDa were recogniz ed by antibodies in sera of naturally infected goats. These sera also recognized up to five molecules ranging from 64-30 kDa, on immunoblots of ammonium sulfate concentrated culture supernatant.