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Vol. 273, Issue 2, 673-676, January 9, 1998
From the Departments of Molecular Biology and Chemistry, The
Scripps Research Institute, La Jolla, California 92037
Virus particles are stable yet exhibit highly
dynamic character given the events that shape their life cycle.
Isolated from their hosts, the nucleoprotein particles are
macromolecules that can be crystallized and studied by x-ray
diffraction. During assembly, maturation and entry, however, they are
highly dynamic and display remarkable plasticity. These dynamic
properties can only be inferred from the x-ray structure and must be
studied by methods that are sensitive to mobility. We have used
matrix-assisted laser desorption/ionization mass spectrometry combined
with time resolved, limited proteolysis (Cohen, S. L.,
Ferre-D'Amare, A. R., Burley, S. K., and Chait, B. T. (1995) Protein Sci. 4, 1088-1099; Kriwacki,
R. W., Wu, J., Tennant, T., Wright, P. E., and Siuzdak,
G. (1997) J. Chromatogr. 777, 23-30; Kriwacki,
R. W., Wu, J., Siuzdak, G., and Wright, P. E. (1996)
J. Am. Chem. Soc. 118, 5320-5321) to examine the viral capsid of flock house virus. Employing less than 10 µg of virus, time course digestion products were assigned to polypeptides of
the subunit. Although surface regions in the three-dimensional structure were susceptible to cleavage on extended exposure to the
protease, the first digestion products were invariably from parts of
the subunit that are internal to the x-ray structure. Regions in the N-
and C-terminal portions of the subunit, located within the shell in the
x-ray structure, but implicated in RNA neutralization and RNA release
and delivery, respectively, were the most susceptible to cleavage
demonstrating transient exposure of these polypeptides to the viral
surface.
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