Three structural polypeptides coded for by minite virus of mice, a parvovirus.

AUTOR(ES)

Tattersall, P

RESUMO

Purified full and empty virions of minute virus of mice were separated on CsCl gradients, and their polypeptides were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The empty particle contains two polypeptides, A (83,300 daltons) and B (64,300 daltons), which are 15 to 18% and 82 to 85%, respectively, of the virion mass. The full particle contains the single-stranded DNA genome, proteins A and B, and a third polypeptide, C (61,400 daltons). Again A is 15 to 18% of the protein mass, but the amounts of B and C vary inversely in different preparations of full particles. These polypeptides comprise greater than 99.6% of the protein in either virion, and their molecular weights and molar ratios are independent of the species of host cell on which the virus is propagated, They are not found in uninfected cells, and no protein component of uninfected cells copurifies with either virion under our conditions. Pulse-chase experiments show that the three proteins are synthesized only after virus infection and are therefore probably virus coded. Sequential harvesting from the nuclei of cells infected under one cycle growth conditions shows an increase in the proportion of C in full particles as infection progresses, suggesting that C is derived from B in a late maturation step.

Documentos Relacionados

• The complete DNA sequence of minute virus of mice, an autonomous parvovirus.
• A precise map of splice junctions in the mRNAs of minute virus of mice, an autonomous parvovirus.
• Structural and nonstructural proteins of a rabbit parvovirus.
• Specific binding sites for a parvovirus, minute virus of mice, on cultured mouse cells.
• Transcription of minute virus of mice, an autonomous parvovirus, may be regulated by attenuation.