title: Caspar carboxylates: the structural basis of tobamovirus disassembly.
abstract: Carboxylate groups have been known for many years to drive the disassembly of simple viruses, including tobacco mosaic virus (TMV). The identities of the carboxylate groups involved and the mechanism by which they initiate disassembly have not, however, been clear. Structures have been determined at resolutions between 2.9 and 3.5 A for five tobamoviruses by fiber diffraction methods. Site-directed mutagenesis has also been used to change numerous carboxylate side chains in TMV to the corresponding amides. Comparison of the stabilities of the various mutant viruses shows that disassembly is driven by a much more complex set of carboxylate interactions than had previously been postulated. Despite the importance of the carboxylate interactions, they are not conserved during viral evolution. Instead, it appears that during evolution, patches of electrostatic interaction drift across viral subunit interfaces. The flexibility of these interactions confers a considerable advantage on the virus, enabling it to change its surface structure rapidly and thus evade host defenses.
authors.affiliation: Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235, USA.
authors.forename: H
authors.initials: H
authors.lastname: Wang
authors.forename: A
authors.initials: A
authors.lastname: Planchart
authors.forename: G
authors.initials: G
authors.lastname: Stubbs
mesh_terms: D001665:Binding Sites; D002213:Capsid / Q000737:chemistry*; D002264:Carboxylic Acids; D046911:Macromolecular Substances; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D055672:Static Electricity; D014027:Tobacco Mosaic Virus / Q000502:physiology / Q000648:ultrastructure; D017898:Tobamovirus / Q000502:physiology* / Q000648:ultrastructure; D019065:Virus Assembly
chemical_list: D002264:Carboxylic Acids; D046911:Macromolecular Substances