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• W3136222140 abstract "The enveloped morbilliviruses utilise conserved proteinaceous receptors to enter host cells: SLAMF1 or Nectin-4. Receptor binding is initiated by the viral attachment protein Haemagglutinin (H), with the viral Fusion protein (F) driving membrane fusion. Crystal structures of the prototypic morbillivirus measles virus H with either SLAMF1 or Nectin-4 are available and have served as the basis for improved understanding of this interaction. However, whether these interactions remain conserved throughout the morbillivirus genus requires further characterisation. Using a random mutagenesis approach, based on error-prone PCR, we targeted the putative receptor binding site for SLAMF1 interaction on peste des petits ruminants virus (PPRV) H, identifying mutations that inhibited virus-induced cell-cell fusion. These data, combined with structural modelling of the PPRV H and ovine SLAMF1 interaction, indicate this region is functionally conserved across all morbilliviruses. Error-prone PCR provides a powerful tool for functionally characterising functional domains within viral proteins." @default.
• W3136222140 created "2021-03-29" @default.
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• W3136222140 date "2021-04-08" @default.
• W3136222140 modified "2023-10-17" @default.
• W3136222140 title "Application of error-prone PCR to functionally probe the morbillivirus Haemagglutinin protein" @default.
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• W3136222140 doi "https://doi.org/10.1099/jgv.0.001580" @default.
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