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Two-dimensional polyacrylamide gel electrophoresis showed that structural virus proteins (VP) were first synthesized in the following time course: VP9 and VP16 during the pulse-labeling period 2-4 h postinfection; VP5 (the major capsid protein), VP23, VP25, and VP39 during the pulse-labeling period 4-6 h postinfection, VP10 and VP41 during the pulse-labeling period 6-8 h postinfection, and VP12 and VP34 during the pulse-labeling period 8-10 h postinfection. Once synthesis began, all of the virus-induced structural proteins, except VP23, were synthesized during the remainder of the one-step virus growth cycle. Synthesis of a nonstructural 45-kilodalton (Kd) virus-induced protein complex began 4-6 h postinfection and continued for the next 20 h. The complex was resolved into two sets of spots, designated the A and B series. The A series consisted of 7 species of proteins with a molecular weight of 45 Kd ranging in isoelectric points from 6.16 to 5.90. The B series consisted of 4 species having a molecular weight of 43.5 Kd and an isoelectric point identical to the homologous protein in the A series. One immediate-early virus-induced protein (VIP115) was identified. Early events in virus infection include selective inhibition of the host protein hgl, glycosylation, and the synthesis of the 45- and 48-Kd virus-induced glycoprotein complexes. The D/E virus-induced protein doublet is synthesized from the infecting virus genome, but its glycosylation is dependent on viral DNA replication.
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Cohrs et al. (1987) studied this question.
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