Ontology highlight
ABSTRACT:
SUBMITTER: Ader N
PROVIDER: S-EPMC3351323 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Ader Nadine N Brindley Melinda A MA Avila Mislay M Origgi Francesco C FC Langedijk Johannes P M JP Örvell Claes C Vandevelde Marc M Zurbriggen Andreas A Plemper Richard K RK Plattet Philippe P
The Journal of biological chemistry 20120319 20
It is unknown how receptor binding by the paramyxovirus attachment proteins (HN, H, or G) triggers the fusion (F) protein to fuse with the plasma membrane for cell entry. H-proteins of the morbillivirus genus consist of a stalk ectodomain supporting a cuboidal head; physiological oligomers consist of non-covalent dimer-of-dimers. We report here the successful engineering of intermolecular disulfide bonds within the central region (residues 91-115) of the morbillivirus H-stalk; a sub-domain that ...[more]