Journal of Virology · 2008 · 79 citations · 14 references
Life SciencesMicrobiologyMolecular BiologyMicrobial GeneticsMolecular VirologyVirologyMembrane FusionViral PathogenesisFusion Protein ActivationFusion Protein MechanismsFusion Regulatory ProteinsHuman Metapneumovirus InfectionViral Fusion Proteins
Membrane fusion promoted by human metapneumovirus (HMPV) fusion (F) protein was suggested to require low pH (R. M. Schowalter, S. E. Smith, and R. E. Dutch, J. Virol. 80:10931-10941, 2006). Using prototype F proteins representing the four HMPV genetic lineages, we detected low-pH-dependent fusion only with some lineage A proteins and not with lineage B proteins. A glycine at position 294 was found responsible for the low-pH requirement in lineage A proteins. Only 6% of all HMPV lineage A F sequences have 294G, and none of the lineage B sequences have 294G. Thus, acidic pH is not a general trigger of HMPV F proteins for activity.
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Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
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