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.
Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.
J P
JP
Sheehan
R M
RM
Iorio
R J
RJ
Syddall
R L
RL
Glickman
M A
MA
Bratt
D000595:Amino Acid Sequence; D001483:Base Sequence; D003545:Cysteine; D015707:HN Protein; D006389:Hemagglutinins, Viral / Q000235:genetics; D008970:Molecular Weight; D009522:Newcastle disease virus / Q000235:genetics; D010084:Oxidation-Reduction; D014759:Viral Envelope Proteins / Q000235:genetics
D015707:HN Protein; D006389:Hemagglutinins, Viral; D014759:Viral Envelope Proteins; D003545:Cysteine