2026-07-23T19:37:08Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/174852024-09-27T19:35:22Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Herfst, Sander
author
Mas-Lloret, Vicente
author
Ver, Lorena S
author
Wierda, Rutger J
author
Osterhaus, Albert D M E
author
Fouchier, Ron A M
author
Melero, Jose Antonio
funder
Unión Europea. Comisión Europea. 5 Programa Marco
funder
Comunidad de Madrid (España)
funder
Ministerio de Educación y Ciencia (España)
2024-02-05T16:43:43Z
2024-02-05T16:43:43Z
2008-09
J Virol. 2008 Sep;82(17):8891-5.
10.1128/JVI.00472-08
1098-5514
Journal of virology
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2519679/pdf/0472-08.pdf
18596097
http://hdl.handle.net/20.500.12105/17485
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.
eng
Low-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenon
research article
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