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Virus Res. 2000 Sep;70(1-2):45-53.

Molecular cloning and expression of human parainfluenza virus type 1 L gene.

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  • 1Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105, USA.


The large (L) protein, a subunit of paramyxovirus RNA polymerase complex is responsible for the majority of enzymic activities involved in viral replication and transcription. To gain insight of the functions of the L protein, we cloned the L gene of human parainfluenza virus type 1 (hPIV1) and sequenced the entire gene. The L gene, which was 6800 nucleotides, encoded a protein of 2223 residues with a calculated molecular weight of 253657. The predicted amino acid sequence was highly homologous with that of Sendai virus (SV) L (86% identity). The hPIV1 L protein expressed from the cloned L gene bound hPIV1 P expressed in the same cells. When cells were transfected with hPIV1 L, P and NP genes together with SV minigenome RNA containing a chloramphenicol acetyltransferase (CAT) gene (Send-CAT), RNA was transcribed, and CAT proteins were detected. These results indicate that the protein encoded by the cloned hPIV1 L gene was biologically functional and that the hPIV1 polymerase complex recognized SV transcription initiation and termination sequences to produce viral transcripts.

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