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Influence of Additional Acylation Site(s) of Influenza B Virus Hemagglutinin on Syncytium Formation
Author(s) -
Ujike Makoto,
Nakajima Katsuhisa,
Nobusawa Eri
Publication year - 2005
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2005.tb03740.x
Subject(s) - mutant , syncytium , hemagglutinin (influenza) , acylation , biology , lipid bilayer fusion , virus , transmembrane domain , fusion , cytoplasm , biophysics , biochemistry , virology , membrane , linguistics , philosophy , gene , catalysis
We studied the effects of an increase in the hydrophobicity of the transmembrane domain (TM) and cytoplasmic tail (CT) of influenza B virus hemagglutinin (BHA) on fusion activities. For this purpose, we created mutant HAs with novel acylation site(s) in the TM and/or CT. All mutants were able to induce hemifusion and to form fusion pores as well as could wild type (wt) BHA. However, the ability of these mutants to form syncytia was impaired, indicating that the increase in the hydrophobicity of these domains (especially the CT) affected fusion pore dilation.