Reducing agent-sensitive dimerization of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus correlates with the presence of cysteine at residue 123.

Viruses within the Newcastle disease virus (NDV) serotype induce a wide array of disease manifestations ranging from an almost apathogenic pattern to the high mortality caused by avirulent or virulent isolates, respectively. A disulfide-linked dimer form of the NDV hemagglutinin-neuraminidase (HN) glycoprotein can be demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions for only some of these isolates. For others, indeed the majority of those we have studied, no such reducing agent-sensitive dimeric form of HN is demonstrable. Apparently, there is no causal relationship between disulfide-linked dimeric HN and virulence. Using the deduced amino acid sequence of the dimeric HN of isolate AV as a basis for selection of oligonucleotide primers, we sequenced three additional reducing agent-sensitive dimeric HN glycoproteins and eight for which a disulfide-linked dimer has not been identified, using primer extension and dideoxy sequencing. The deduced amino acid sequences reveal a strict correlation between the presence of cysteine at residue 123 and reducing agent-sensitive dimerization of HN.