Conformational flexibility and polymerization of vesicular stomatitis virus matrix protein.
The matrix protein of vesicular stomatitis virus (VSV) plays a pivotal role in viral assembly. We previously demonstrated the ability of M protein to self-associate at low salt concentrations. Now, we show the ability of M protein to polymerize in the presence of ZnCl2 in a nucleation-dependent manner. Analysis of kinetics revealed that the nuclei are probably made of three or four molecules of M. These results are consistent with the idea that in vitro self association of M protein is not due to amorphous aggregation but rather reflects an intrinsic ability of M to polymerize. Using attenuated total reflectance Fourier transform infrared spectroscopy, we showed that M polymerization is associated with an increase in the beta-sheet content of the protein. We propose a model explaining both the apparent M protein solubility in infected cells and how M polymerization could promote viral assembly. Data available for other negative strand viruses suggest that M polymerization may be the general basis of viral assembly.
Gaudin
Y
Y
Laboratoire de génétique des virus du CNRS, 91198 Gif sur Yvette cedex, France.
Sturgis
J
J
Doumith
M
M
Barge
A
A
Robert
B
B
Ruigrok
R W
RW
D002712:Chlorides; D007700:Kinetics; D008027:Light; D009994:Osmolar Concentration; D011108:Polymers; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation; D012965:Sodium Chloride; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D014721:Vesicular stomatitis Indiana virus / Q000737:chemistry* / Q000502:physiology; D014763:Viral Matrix Proteins / Q000737:chemistry*; D019065:Virus Assembly / Q000502:physiology; D017967:Zinc Compounds
D002712:Chlorides; C094460:M protein, Vesicular stomatitis virus; D011108:Polymers; D014763:Viral Matrix Proteins; D017967:Zinc Compounds; D012965:Sodium Chloride; C016837:zinc chloride