A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion

Molecular Biology of the Cell

Volumn 11, Issue 11, 2000, Pages 3765-3775

  Melikyan, G B ^a   Markosyan, R M ^a   Roth, M G ^a   Cohen, F S ^a  

^a RUSH MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORPROMAZINE; HEMAGGLUTININ; LIPID; PROTEINASE K;

ARTICLE; CHANNEL GATING; CONTROLLED STUDY; INFLUENZA VIRUS; MEMBRANE FUSION; MOLECULAR STABILITY; NONHUMAN; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; TEMPERATURE DEPENDENCE; VIRUS MUTATION;

INFLUENZA VIRUS; RNA VIRUSES;

EID: 0033730718     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.11.3765     Document Type: Article

References (31)

1. Structural basis for paramyxovirus-mediated membrane fusion
2. Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion: A new model for fusion
3. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil
4. Lipids in biological membrane fusion
5. The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
6. An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids
7. Membrane fusion activity of the influenza virus hemagglutinin: The low pH-induced conformational change
8. Phase tracking: An improved phase detection technique for cell membrane capacitance measurements
9. Multiple local contact sites are induced by GPI-linked influenza hemagglutinin during hemifusion and flickering pore formation
10. Cell-surface expression of influenza hemagglutinin from a cloned DNA copy of the RNA gene
11. Pores formed by influenza hemagglutinin
12. Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusion
13. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
14. The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
15. Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion
16. Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion
17. Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
18. Role of the cytoplasmic tail of ecotropic Moloney murine leukemia virus Env protein in fusion pore formation
19. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
20. Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells: Measurement by dequenching of fluorescence
21. SV40 virus expression vectors
22. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
23. Fusion pore conductance: Experimental approaches and theoretical algorithms
24. Effects of spontaneous bilayer curvature on influenza virus-mediated fusion pores
25. Interaction of influenza virus hemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
26. Coiled coils in both intracellular vesicle and viral membrane fusion
27. Patch clamp studies of single cell-fusion events mediated by a viral fusion protein
28. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin
29. The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion
30. Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion
31. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion