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Gene Review:

L - RNA polymerase

Human parainfluenza virus 1

McAuliffe, J.M. et al., Bousse, T. et al., Grogan, C.C. et al.

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Disease relevance of L

Codon substitution mutations at two positions in the L polymerase protein of human parainfluenza virus type 1 yield viruses with a spectrum of attenuation in vivo and increased phenotypic stability in vitro [1].
Sendai virus wild-type and mutant C proteins show a direct correlation between L polymerase binding and inhibition of viral RNA synthesis [2].

High impact information on L

The Y942H and L992F temperature-sensitive (ts) and attenuating amino acid substitution mutations, previously identified in the L polymerase of the HPIV3cp45 vaccine candidate, were introduced into homologous positions of the L polymerase of recombinant human parainfluenza virus type 1 (rHPIV1) [1].
Mutant SV P or hPIV1 P cDNAs, which do not express C proteins, showed the same phenotype with wild-type P cDNAs, indicating that C proteins are not responsible for the dysfunction of SV P--hPIV1 L polymerase complex [3].

References

Codon substitution mutations at two positions in the L polymerase protein of human parainfluenza virus type 1 yield viruses with a spectrum of attenuation in vivo and increased phenotypic stability in vitro. McAuliffe, J.M., Surman, S.R., Newman, J.T., Riggs, J.M., Collins, P.L., Murphy, B.R., Skiadopoulos, M.H. J. Virol. (2004) [Pubmed]
Sendai virus wild-type and mutant C proteins show a direct correlation between L polymerase binding and inhibition of viral RNA synthesis. Grogan, C.C., Moyer, S.A. Virology (2001) [Pubmed]
Two regions of the P protein are required to be active with the L protein for human parainfluenza virus type 1 RNA polymerase activity. Bousse, T., Takimoto, T., Matrosovich, T., Portner, A. Virology (2001) [Pubmed]

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