Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6140712 | Virology | 2013 | 11 Pages |
â¢Paramyxoviral phosphoproteins are known to oligomerize through coiled-coils.â¢All paramyxoviral phosphoproteins studied so far are tetramers.â¢We purified and characterized the Nipah virus P protein multimerization domain (PMD).â¢We show that PMD forms a very stable and elongated coiled-coil trimer.â¢This is the first report of a Paramyxoviridae P protein forming trimers.
Nipah virus (NiV) is a recently emerged severe human pathogen that belongs to the Henipavirus genus within the Paramyxoviridae family. The NiV genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid that is the substrate used by the polymerase for transcription and replication. The polymerase is recruited onto the nucleocapsid via its cofactor, the phosphoprotein (P). The NiV P protein has a modular organization, with alternating disordered and ordered domains. Among these latter, is the P multimerization domain (PMD) that was predicted to adopt a coiled-coil conformation. Using both biochemical and biophysical approaches, we show that NiV PMD forms a highly stable and elongated coiled-coil trimer, a finding in striking contrast with respect to the PMDs of Paramyxoviridae members investigated so far that were all found to tetramerize. The present results therefore represent the first report of a paramyxoviral P protein forming trimers.