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Rhabdovirus Matrix Protein Structures Reveal a Novel Mode of Self-Association

DOI: 10.1371/journal.ppat.1000251 DOI Help
PMID: 19112510 PMID Help

Authors: Stephen Graham (University of Cambridge) , Rene Assenburg (Wellcome Trust Centre for Human Genetics, University of Oxford) , Olivier Delmas (WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris,) , Anil Verma (Research Complex at Harwell) , Alireza Gholami (WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France) , Chiraz Talbi (WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, Paris, France) , Ray Owens (University of Oxford) , Dave Stuart (Diamond Light Source) , Jonathan Grimes (Division of Structural Biology, University of Oxford) , Herve Bourhy (Wellcome Trust Centre for Human Genetics, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Plos Pathogens , VOL 4 (12)

State: Published (Approved)
Published: December 2008

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials

Facility: ESRF