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Journal of Virology, August 2002, p. 8101-8109, Vol. 76, No. 16
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.16.8101-8109.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Role of a Highly Conserved NH₂-Terminal Domain of the Human Parainfluenza Virus Type 3 RNA Polymerase

Achut G. Malur, Suresh K. Choudhary, Bishnu P. De,^, and Amiya K. Banerjee^*

Department of Virology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195

Received 29 March 2002/ Accepted 23 May 2002

The RNA polymerase complex of human parainfluenza virus type 3 (HPIV 3), a member of the family Paramyxoviridae, is composed of two virally encoded polypeptides: a multifunctional large protein (L, 255 kDa) and a phosphoprotein (P, 90 kDa). From extensive deduced amino acid sequence analyses of the cDNA clones of a number of L proteins of nonsegmented negative-strand RNA viruses, a cluster of high-homology sequence segments have been identified within the body of the L proteins. Here, we have focused on the NH₂-terminal domain of HPIV 3 L protein that is also highly conserved. Following mutational analyses within this domain, we examined the ability of the mutant L proteins to (i) transcribe an HPIV 3 minireplicon, (ii) transcribe the viral RNA in vitro using the HPIV 3 nucleocapsid RNA template, and (iii) interact with HPIV 3 P protein. Our results demonstrate that the first 15 amino acids of the NH₂-terminal domain spanning a highly conserved motif is directly involved in transcription of the genome RNA and in forming a functional complex with the P protein. Substitution of eight nonconserved amino acids within this domain by the corresponding Sendai virus L protein residues yielded mutants with variable transcriptional activities. However, one mutant in which all eight amino acids were replaced with the corresponding residues of Sendai virus L protein failed to both transcribe the minireplicon and interact with HPIV 3 P and the Sendai virus P protein. The possible functional significance of the NH₂-terminal domain of paramyxovirus L protein is discussed.

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* Corresponding author. Mailing address: Department of Virology NN1-10, Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Phone: (216) 444-0625. Fax: (216) 444-2998. E-mail: banerja{at}ccf.org.

Present address: Department of Genetic Medicine, Weill Medical College, Cornell University, New York, NY 10021.

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Journal of Virology, August 2002, p. 8101-8109, Vol. 76, No. 16
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.16.8101-8109.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

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