Rhabdovirus matrix protein structures reveal a novel mode of self-association.

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.

journal_name

PLoS Pathog

journal_title

PLoS pathogens

authors

Graham SC,Assenberg R,Delmas O,Verma A,Gholami A,Talbi C,Owens RJ,Stuart DI,Grimes JM,Bourhy H

doi

10.1371/journal.ppat.1000251

subject

Has Abstract

pub_date

2008-12-01 00:00:00

pages

e1000251

issue

12

eissn

1553-7366

issn

1553-7374

journal_volume

4

pub_type

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