The shape of purified matrix protein (M) of vesicular stomatitis virus
was determined using biophysical techniques like analytical centrifug
ation, dynamic light scattering, and small-angle neutron scattering. T
he data obtained are consistent with a rod-like model for M protein wi
th a length of about 100 +/- 10 Angstrom and a radius of 9 +/- 1 Angst
rom. These dimensions are in agreement with the substructure of M prot
ein aggregates and with the fine morphology of the axial channel mater
ial found inside the viral nucleocapsid coil. This morphological infor
mation was combined with Co measurements and secondary structure predi
ctions on four vesiculovirus M proteins leading to a proposal for the
structure of M protein. (C) 1996 Academic Press, Inc.