Phase diagram of self-assembled viral capsid protein polymorphs.
We present an experimental study of the self-assembly of capsid proteins of the cowpea chlorotic mosaic virus (CCMV), in the absence of the viral genome, as a function of pH and ionic strength. In accord with previous measurements, a wide range of polymorphs can be identified by electron microscopy, among them single and multiwalled shells and tubes. The images are analyzed with respect to size and shape of aggregates, and evidence is given that equilibrium has been achieved, allowing a phase diagram to be constructed. Some previously unreported structures are also described. The range and stability of the polymorphs can be understood in terms of electrostatic interactions and the way they affect the spontaneous curvature of protein networks and the relative stabilities of pentamers and hexamers.
Lavelle
L
L
Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095-1569, USA.
Gingery
M
M
Phillips
M
M
Gelbart
W M
WM
Knobler
C M
CM
Cadena-Nava
R D
RD
Vega-Acosta
J R
JR
Pinedo-Torres
L A
LA
Ruiz-Garcia
J
J
D017795:Bromovirus / Q000737:chemistry*; D036022:Capsid Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D010316:Particle Size; D044367:Phase Transition; D011487:Protein Conformation; D055672:Static Electricity; D013499:Surface Properties; D013816:Thermodynamics
D036022:Capsid Proteins