Acylation of the influenza hemagglutinin modulates fusion activity

被引:36
作者
Fischer, C
Schroth-Diez, B
Herrmann, A
Garten, W
Klenk, HD
机构
[1] Philipps Univ Marburg, Inst Virol, D-35011 Marburg, Germany
[2] Humboldt Universitat Berlin, Math Naturwissenschaftliche Fak 1, Inst Biol Biophys, D-10115 Berlin, Germany
关键词
D O I
10.1006/viro.1998.9286
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The influenza virus hemagglutinin (HA) contains three highly conserved cysteine residues at positions 551, 559, and 562 close to the carboxyl-terminus of the HA2 subunit which serve as palmitylation sites. Wild-type HA of influenza virus A/FPV/Rostock/34 (H7N1) and HA permutated by exchange of the acylated cysteine to serine residues were expressed in CV-1 cells by a SV40 vector system. Since density of immunostained HA on the cell surface measured by flow cytometric analysis did not differ between wild-type and acylation mutants, it was possible to compare acylation mutants and wild-type HA for their capacity to induce membrane fusion at low pH. The following observations were made: (1) lateral diffusion of a lipid-like fluorophore (R-18) from the erythrocyte membrane to the plasma membrane of cells expressing HA on the surface occured equally well with mutants and wild type. (2) Diffusion of a low-molecular-weight fluorescent water-soluble probe (calcein) from erythrocytes into the cytoplasm of HA-expressing cells was not altered either. (3) However, depending on the position and the number of the deleted acylation sites, the mutants showed a reduced ability to induce syncytia. The data indicate that deacylation of the cytoplasmic tail has no measurable effect on the capacity of HA to induce membrane fusion and pore formation but that it suppresses syncytia formation. (C) 1998 Academic Press.
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页码:284 / 294
页数:11
相关论文
共 44 条
[1]   Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events [J].
Blumenthal, R ;
Sarkar, DP ;
Durell, S ;
Howard, DE ;
Morris, SJ .
JOURNAL OF CELL BIOLOGY, 1996, 135 (01) :63-71
[2]   STRUCTURE OF INFLUENZA HEMAGGLUTININ AT THE PH OF MEMBRANE-FUSION [J].
BULLOUGH, PA ;
HUGHSON, FM ;
SKEHEL, JJ ;
WILEY, DC .
NATURE, 1994, 371 (6492) :37-43
[3]   A SPRING-LOADED MECHANISM FOR THE CONFORMATIONAL CHANGE OF INFLUENZA HEMAGGLUTININ [J].
CARR, CM ;
KIM, PS .
CELL, 1993, 73 (04) :823-832
[4]   DELAY TIME FOR INFLUENZA-VIRUS HEMAGGLUTININ-INDUCED MEMBRANE-FUSION DEPENDS ON HEMAGGLUTININ SURFACE-DENSITY [J].
CLAGUE, MJ ;
SCHOCH, C ;
BLUMENTHAL, R .
JOURNAL OF VIROLOGY, 1991, 65 (05) :2402-2407
[5]   Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers [J].
Danieli, T ;
Pelletier, SL ;
Henis, YI ;
White, JM .
JOURNAL OF CELL BIOLOGY, 1996, 133 (03) :559-569
[6]   FUSION MUTANTS OF THE INFLUENZA-VIRUS HEMAGGLUTININ GLYCOPROTEIN [J].
DANIELS, RS ;
DOWNIE, JC ;
HAY, AJ ;
KNOSSOW, M ;
SKEHEL, JJ ;
WANG, ML ;
WILEY, DC .
CELL, 1985, 40 (02) :431-439
[7]   FUSION OF INFLUENZA HEMAGGLUTININ-EXPRESSING FIBROBLASTS WITH GLYCOPHORIN-BEARING LIPOSOMES - ROLE OF HEMAGGLUTININ SURFACE-DENSITY [J].
ELLENS, H ;
BENTZ, J ;
MASON, D ;
ZHANG, F ;
WHITE, JM .
BIOCHEMISTRY, 1990, 29 (41) :9697-9707
[8]   Retrovirus envelope domain at 1.7 angstrom resolution [J].
Fass, D ;
Harrison, SC ;
Kim, PS .
NATURE STRUCTURAL BIOLOGY, 1996, 3 (05) :465-469
[9]   STRUCTURE AND ASSEMBLY OF HEMAGGLUTININ MUTANTS OF FOWL PLAGUE VIRUS WITH IMPAIRED SURFACE TRANSPORT [J].
GARTEN, W ;
WILL, C ;
BUCKARD, K ;
KURODA, K ;
ORTMANN, D ;
MUNK, K ;
SCHOLTISSEK, C ;
SCHNITTLER, H ;
DRENCKHAHN, D ;
KLENK, HD .
JOURNAL OF VIROLOGY, 1992, 66 (03) :1495-1505
[10]   STUDIES ON THE MECHANISM OF MEMBRANE-FUSION - SITE-SPECIFIC MUTAGENESIS OF THE HEMAGGLUTININ OF INFLUENZA-VIRUS [J].
GETHING, MJ ;
DOMS, RW ;
YORK, D ;
WHITE, J .
JOURNAL OF CELL BIOLOGY, 1986, 102 (01) :11-23