In vitro synthesis and assembly of picornaviral capsid intermediate structures.

AUTOR(ES)

Palmenberg, A C

RESUMO

Cell-free translation of encephalomyocarditis RNA in extracts of rabbit reticulocytes results in the synthesis of viral proteins indistinguishable from those produced during virus infection of cells. The viral capsid proteins are produced in an active form capable of assembly into viral capsid intermediate structures. Protomers (5S), pentamers (14S), and shell-like structures (75 to 85S) can be detected after prolonged incubation in the extracts. Proteolytic cleavage of capsid precursor proteins appears to be a prerequisite for assembly, in apparent contrast to cell-associated assembly. Assembly of pentamers is also preceded by conversion of protein epsilon 1 to epsilon in a step which may reflect an amino-terminal blocking reaction.

Documentos Relacionados

• Picornaviral capsid assembly: similarity of rhinovirus and enterovirus precursor subunits.
• Self-assembly of biological structures.
• Membrane subunits of Mycoplasma laidlawii and their assembly to membranelike structures.
• Picornaviral structure and assembly.
• Fibril assembly and carotenoid overaccumulation in chromoplasts: a model for supramolecular lipoprotein structures.