Influence of additional acylation site(s) of influenza B virus hemagglutinin on syncytium formation.
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.
Ujike
Makoto
M
Department of Microbiology and Infection, Nagoya City University Graduate School of Medical Science, Nagoya, Aichi 467-8601, Japan.
Nakajima
Katsuhisa
K
Nobusawa
Eri
E
D000215:Acylation; D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D015726:Giant Cells / Q000502:physiology*; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D009981:Influenza B virus / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D008561:Membrane Fusion; D009154:Mutation
D019267:Hemagglutinin Glycoproteins, Influenza Virus