| Type |
Article |
| Date |
2008 |
| Language |
English |
| Author(s) |
Graham Stephen C.1, Assenberg René1, Delmas Olivier2, Verma Anil1, Gholami Alireza2, Talbi Chiraz2, Owens Raymond J.1, Stuart David I.1, Grimes Jonathan M.1, Bourhy Hervé2 |
| Affiliation(s) |
1 : Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom
2 : UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France |
| Source |
PLOS pathogens (1553-7374) (Public Library Science), 2008 , Vol. 4 , N. 12 , P. 1-12 |
| DOI |
10.1371/journal.ppat.1000251 |
| Abstract |
The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins. |
| Full Text |
| File |
Pages |
Size |
Access |
| Publisher's official version |
12 |
935 KB |
Open access |
|
