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

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). In r...

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Bibliographic Details
Published in:	J Virol
Main Authors:	McAuliffe, Josephine M., Surman, Sonja R., Newman, Jason T., Riggs, Jeffrey M., Collins, Peter L., Murphy, Brian R., Skiadopoulos, Mario H.
Format:	Artigo
Language:	Inglês
Published:	American Society for Microbiology (ASM) 2004
Subjects:	Vaccines and Antiviral Agents
Online Access:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC369445/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14747567/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JVI.78.4.2029-2036.2004
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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

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