Conformational flexibility and polymerization of vesicular stomatitis virus matrix protein.

Abstract:

: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.

journal_name

J Mol Biol

authors

Gaudin Y,Sturgis J,Doumith M,Barge A,Robert B,Ruigrok RW

doi

10.1006/jmbi.1997.1439

subject

Has Abstract

pub_date

1997-12-19 00:00:00

pages

816-25

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(97)91439-X

journal_volume

274

pub_type

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