Abstract
Ts101, a mutant of WSN influenza virus, has a temperature-sensitive lesion in P1, a structural protein of the virion. P1 is required for cRNA synthesis, and no detectable cRNA is synthesized by ts101 in infected cells at the nonpermissive temperature. In the present study, the virion transcriptase activity of ts101 is shown to be temperature-sensitive in vitro, but only at low concentrations of the dinucleotide primer ApG, which is required specifically for initiation. At saturating concentrations of ApG, ts101 was not distinguishable from ts+. It is suggested that P1 is required for initiation of transcription, and normally functions in vivo in the recognition of the putative physiological primer. Inasmuch as P1 and P3 are known to be the only gene products which are required for the synthesis of viral cRNA, it seems likely that P3 functions in the elongation process.
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