Rod-like shape of vesicular stomatitis virus matrix protein

Abstract

The shape of purified matrix protein (M) of vesicular stomatitis virus was determined using biophysical techniques like analytical centrifugation, dynamic light scattering, and small-angle neutron scattering. The data obtained are consistent with a rod-like model for M protein with a length of about 100 ± 10 Å and a radius of 9 ± 1 Å. These dimensions are in agreement with the substructure of M protein aggregates and with the fine morphology of the axial channel material found inside the viral nucleocapsid coil. This morphological information was combined with CD measurements and secondary structure predictions on four vesiculovirus M proteins leading to a proposal for the structure of M protein.