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J Gen Virol 76 (1995), 2081-2084; DOI 10.1099/0022-1317-76-8-2081
© 1995 Society for General Microbiology
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Elongation activity of poliovirus RNA polymerase derived from Sabin type 1 sequence is not temperature sensitive

Susan Baker, Oliver C. Richards and Ellie Ehrenfeld*

Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, California 92717, USA

Determinants of attenuation in the Sabin type 1 strain of poliovirus are located in the 5' noncoding region, the capsid coding region and the viral RNA-dependent RNA polymerase (3Dpol) coding region. These mutations also contribute to a temperature sensitive phenotype of virus replication. We have cloned and expressed the Sabin 1 virus 3Dpol protein which contains three amino acid differences from the wild-type (Mahoney) sequence, as well as a wild-type polymerase containing only a single Sabin amino acid substitution at nt 6203. These enzymes have been examined and compared for temperature sensitive polymerase activity. Wild-type and mutated polymerases demonstrated identical specific activities at 30, 35 and 39 °C. All three showed the same kinetics of heat inactivation after pre-incubation at elevated temperatures. Thus the contribution of Sabin 3Dpol sequences to the inability of the virus to grow at elevated temperatures must lie in a function or activity of the enzyme other than RNA polymerization. A likely reaction is the initiation step of RNA chain synthesis.

* Author for correspondence. Fax +1 714 824 8551. e-mail EEHRENFE@UCI.edu

Received 19 January 1995; accepted 21 April 1995.




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Copyright © 1995 by the Society for General Microbiology.