Physical regulation of the self-assembly of tobacco mosaic virus coat protein.
We present a statistical mechanical model based on the principle of mass action that explains the main features of the in vitro aggregation behavior of the coat protein of tobacco mosaic virus (TMV). By comparing our model to experimentally obtained stability diagrams, titration experiments, and calorimetric data, we pin down three competing factors that regulate the transitions between the different kinds of aggregated state of the coat protein. These are hydrophobic interactions, electrostatic interactions, and the formation of so-called "Caspar" carboxylate pairs. We suggest that these factors could be universal and relevant to a large class of virus coat proteins.
Kegel
Willem K
WK
Van't Hoff Laboratory for Physical and Colloid Chemistry, Debye Research Institute, Utrecht University, Utrecht, The Netherlands. w.k.kegel@chem.uu.nl
van der Schoot
Paul
P
D001665:Binding Sites; D036022:Capsid Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D003460:Crystallization / Q000379:methods*; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000648:ultrastructure*; D011485:Protein Binding; D011487:Protein Conformation; D014027:Tobacco Mosaic Virus / Q000737:chemistry*; D019065:Virus Assembly
D036022:Capsid Proteins; D046912:Multiprotein Complexes