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Biophys J, July 2001, p. 586-594, Vol. 81, No. 1
and
Departments of *Molecular Genetics & Microbiology,
Chemistry, and Physiology & Biophysics,
State University of New York at Stony Brook, Stony Brook, New York
11794 USA
The viral genome and replicative enzymes of the human
immunodeficiency virus are encased in a shell consisting of assembled mature capsid protein (CA). The core shell is a stable, effective protective barrier, but is also poised for dissolution on cue to allow
transmission of the viral genome into its new host. In this study,
static light scattering (SLS) and dynamic light scattering (DLS) were
used to examine the entire range of the CA protein response to an
environmental cue (pH). The CA protein assembled tubular structures as
previously reported but also was capable of assembling spheres,
depending on the pH of the protein solution. The switch from formation
of one to the other occurred within a very narrow physiological pH
range (i.e., pH 7.0 to pH 6.8). Below this range, only dimers were
detected. Above this range, the previously described tubular structures
were detected. The ability of the CA protein to form a spherical
structure that is detectable by DLS but not by electron microscopy
indicates that some assemblages are inherently sensitive to
perturbation. The dimers in equilibrium with these assemblages
exhibited distinct conformations: Dimers in equilibrium with the
spherical form exhibited a compact conformation. Dimers in equilibrium
with the rod-like form had an extended conformation. Thus, the CA
protein possesses the inherent ability to form metastable structures,
the morphology of which is regulated by an environmentally-sensitive
molecular switch. Such metastable structures may exist as transient
intermediates during the assembly and/or disassembly of the virus core.
Biophys J, July 2001, p. 586-594, Vol. 81, No. 1
© 2001 by the Biophysical Society 0006-3495/01/07/586/09 $2.00
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