Herfst, SanderMas-Lloret, VicenteVer, Lorena SWierda, Rutger JOsterhaus, Albert D M EFouchier, Ron A MMelero, Jose Antonio2024-02-052024-02-052008-09J Virol. 2008 Sep;82(17):8891-5.https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2519679/pdf/0472-08.pdfhttp://hdl.handle.net/20.500.12105/17485Membrane 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.engVoRhttp://creativecommons.org/licenses/by-nc-nd/4.0/AnimalsChlorocebus aethiopsHumansHydrogen-Ion ConcentrationMembrane FusionMetapneumovirusModels, MolecularPhylogenyProtein ConformationProtein Structure, SecondaryVero CellsViral Fusion ProteinsLow-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenonAttribution-NonCommercial-NoDerivatives 4.0 Internacional1859609782178891-889510.1128/JVI.00472-081098-5514Journal of virologyopen access