title: Conformational change of rubella virus spike proteins induced by 2-mercaptoethanol.
abstract: Hemagglutinating (HA) activity of rubella virus was inactivated with 2-mercaptoethanol (2ME) in a dose-dependent manner. But even low concentrations of 2ME, which had little effect on HA activity by themselves, greatly increased the sensitivity of spike polypeptides to the subsequent trypsin treatment. Increased trypsin sensitivity was shown by an enhanced reduction of HA activity and an enhanced proteolytic removal of both E1 and E2 polypeptides from the surface of the virion. The findings indicate that 2ME causes an extensive disruption in the conformation of spikes composed of E1 and E2 polypeptides.
authors.affiliation: Department of Measles Virus, National Institute of Health, Tokyo.
authors.forename: S
authors.initials: S
authors.lastname: Katow
authors.forename: A
authors.initials: A
authors.lastname: Sugiura
mesh_terms: D000818:Animals; D006224:Cricetinae; D004586:Electrophoresis; D006023:Glycoproteins / Q000302:isolation & purification; D006387:Hemagglutination, Viral / Q000187:drug effects; D008623:Mercaptoethanol / Q000494:pharmacology*; D011233:Precipitin Tests; D011487:Protein Conformation / Q000187:drug effects*; D011489:Protein Denaturation; D012412:Rubella virus / Q000032:analysis / Q000187:drug effects*; D014357:Trypsin / Q000378:metabolism; D014764:Viral Proteins / Q000302:isolation & purification
chemical_list: D006023:Glycoproteins; D014764:Viral Proteins; D008623:Mercaptoethanol; D014357:Trypsin