Crystal structure of vesicular stomatitis virus matrix protein.
The vesicular stomatitis virus (VSV) matrix protein (M) interacts with cellular membranes, self-associates and plays a major role in virus assembly and budding. We present the crystallographic structure, determined at 1.96 A resolution, of a soluble thermolysin resistant core of VSV M. The fold is a new fold shared by the other vesiculovirus matrix proteins. The structure accounts for the loss of stability of M temperature-sensitive mutants deficient in budding, and reveals a flexible loop protruding from the globular core that is important for self-assembly. Membrane floatation shows that, together with the M lysine-rich N-terminal peptide, a second domain of the protein is involved in membrane binding. Indeed, the structure reveals a hydrophobic surface located close to the hydrophobic loop and surrounded by conserved basic residues that may constitute this domain. Lastly, comparison of the negative-stranded virus matrix proteins with retrovirus Gag proteins suggests that the flexible link between their major membrane binding domain and the rest of the structure is a common feature shared by these proteins involved in budding and virus assembly.
Gaudier
Martin
M
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif sur Yvette Cedex, France.
Gaudin
Yves
Y
Knossow
Marcel
M
D000595:Amino Acid Sequence; D000818:Animals; D006224:Cricetinae; D008081:Liposomes / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D014721:Vesicular stomatitis Indiana virus / Q000737:chemistry; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000235:genetics
D008081:Liposomes; C094460:M protein, Vesicular stomatitis virus; D014763:Viral Matrix Proteins