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Influence of additional acylation site(s) of influenza B virus hemagglutinin on syncytium formation.
- Source :
-
Microbiology and immunology [Microbiol Immunol] 2005; Vol. 49 (4), pp. 355-9. - Publication Year :
- 2005
-
Abstract
- 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.
- Subjects :
- Acylation
Animals
COS Cells
Chlorocebus aethiops
Hemagglutinin Glycoproteins, Influenza Virus genetics
Hemagglutinin Glycoproteins, Influenza Virus metabolism
Hydrophobic and Hydrophilic Interactions
Influenza B virus metabolism
Influenza B virus physiology
Mutation
Giant Cells physiology
Hemagglutinin Glycoproteins, Influenza Virus chemistry
Influenza B virus chemistry
Membrane Fusion
Subjects
Details
- Language :
- English
- ISSN :
- 0385-5600
- Volume :
- 49
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Microbiology and immunology
- Publication Type :
- Academic Journal
- Accession number :
- 15840961
- Full Text :
- https://doi.org/10.1111/j.1348-0421.2005.tb03740.x