Open AccessLow-pH-Induced Membrane Fusion Mediated by Human Metapneumovirus F Protein Is a Rare, Strain-Dependent Phenomenon
Author(s) -
Sander Herfst,
Vicente Más,
Lorena S. Ver,
Rutger J. Wierda,
Albert D. M. E. Osterhaus,
Ron A. M. Fouchier,
José A. Melero
Publication year - 2008
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00472-08
Subject(s) - human metapneumovirus , lineage (genetic) , biology , metapneumovirus , lipid bilayer fusion , virology , strain (injury) , fusion protein , genetics , virus , gene , respiratory system , respiratory tract infections , recombinant dna , anatomy
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.