Functional aspects of the capsid structure of Mengo virus.
The three-dimensional structure of the Mengo virus capsid has been determined at a resolution of 3.0 A. This achievement is discussed in an historical context, and the general features of picornavirus capsid design are presented. The dynamic functional aspects of the Mengo virus capsid--namely its ability to interact with specific receptors on host cells, to dissociate and release the viral genomic RNA into the cellular cytoplasm, to assemble with progeny RNA molecules and form new virions, and to alter its external surface in order to evade neutralization by circulating antibodies--are discussed. Comparisons with other picornaviruses whose capsid structures have also been elucidated (poliovirus serotype 1 and 3, human rhinovirus types 14 and 1A, and foot-and-mouth disease virus type O) illustrate both the similarities and the distinctive features of capsid design found within this family of mammalian viruses.
Scraba
D G
DG
Department of Biochemistry, University of Alberta, Edmonton, Canada.
D000818:Animals; D002213:Capsid / Q000648:ultrastructure*; D008574:Mengovirus / Q000648:ultrastructure*; D008854:Microscopy, Electron; D008961:Models, Structural; D010849:Picornaviridae / Q000502:physiology / Q000648:ultrastructure; D011991:Receptors, Virus / Q000502:physiology; D014771:Virion / Q000648:ultrastructure; D014961:X-Ray Diffraction
D011991:Receptors, Virus