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1 Unité de Virologie Moléculaire (CNRS UA 545), Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris Cedex 15, France,
2 A. N. Belozersky Institute of Physical Chemical Biology, Moscow State University, 119899 Moscow, Russia
and3 Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region, Russia
The amino acid sequence of the poliovirus 2C protein contains two highly conserved stretches, GSPGTGKS136 and MDD177, which correspond to the consensus ‘A’ and ‘B’ motifs (GXXXXGKS/T and DD/E, respectively) found in nucleoside triphosphate-binding proteins. To assess the functional importance of these amino acid sequences, we changed conserved and non-conserved amino acids. The replacement of the non-conserved Thr133 residue with Ser or Ala did not markedly change the virus phenotype. Similarly, replacement of the non-conserved Pro131 residue by Ala did not abolish virus viability, but changes of this residue to Thr or Asn were not tolerated. No viable mutant could be isolated after transfection of cultured cells with transcripts mutated at the conserved Lys135, Ser136 or Asp177 residues. However, true revertants were selected from Arg135 and Ser135 mutants, from Glu177 and Gly177 mutants, and from Ala136 mutants. Thr136 mutants not only gave rise to true revertants, but also to two independent isolates of a suppressor mutant, Asn140
Tyr. All the lethal mutations resulted in severe inhibition of viral RNA synthesis in vivo, although no translational deficiency was detected in a cell-free system. This is the first direct evidence for the functional significance of the nucleoside triphosphatebinding pattern in the poliovirus 2C protein.
Permanent address: A. N. Belozersky Institute of Physical Chemical Biology, Moscow State University, 119899 Moscow, Russia.
Received 5 February 1992;
accepted 6 May 1992.
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