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SUMMARY Dithiothreitol (DTT), a reagent which cleaves disulphide bonds, destroyed the haemagglutinin, neuraminidase and 'haemolysin' of Sendal virus. The treated virus particles appeared morphologically intact. They failed to bind haemag- glutination-inhibiting (HI) and neuraminidase-inhibiting (NI) antibodies. Anti- sera against DTT-treated virus inhibited haemolysis induced by intact virus, although they did not contain detectable HI, NI or virus-neutralizing antibodies. Treated and untreated virus particles were labelled with (14C)-iodoacetamide or with (14C)-N-ethylmaleimide, disrupted with SDS and subsequently electrophoresed in polyacrylamide gels. Thus, polypeptide species with accessible cysteinyl residues, either originally present in intact virus or resulting from reduction of disulphide bonds, were distinguished. The significance of these findings is discussed.

Virocidal Cleavage of Disulphide Bonds within Structural Proteins of Sendai Virus