Viral fusion peptides: A tool set to disrupt and connect biological membranes

Bioscience Reports

Volumn 20, Issue 6, 2000, Pages 501-518

  Tamm, Lukas K ^a   Han, Xing ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

Amyloid peptide; Conformational change; HIV gp41; Host guest peptide; Influenza haemagglutinin; Lipid protein interaction; Membrane fusion; Membrane protein folding; Secondary structure; Thermodynamics; Viral fusion peptide

Indexed keywords

VIRUS FUSION PROTEIN;

CELL FUSION; HUMAN IMMUNODEFICIENCY VIRUS; INFLUENZA VIRUS; NONHUMAN; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN LIPID INTERACTION; PROTEIN SECONDARY STRUCTURE; SHORT SURVEY; VIRUS CELL INTERACTION;

AMINO ACID SEQUENCE; MEMBRANE FUSION; MOLECULAR SEQUENCE DATA; VIRAL FUSION PROTEINS;

HUMAN IMMUNODEFICIENCY VIRUS; INFLUENZA VIRUS;

EID: 0034444121     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010406920417     Document Type: Article

References (56)

1. The transmembrane domain of the influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
2. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
3. Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins
4. Structure of influenza haemagglutinin at the pH of membrane fusion
5. Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: Importance of interbilayer separation
6. A spring-loaded mechanism for the conformational change of influenza hemagglutinin
7. 2 subunit to form an N cap that terminates the triple-stranded coiled coil
8. Lipids in biological membrane fusion
9. Empirical predictions of protein conformation
10. Design of membrane-inserting peptides: Spectroscopic characterization with and without lipid bilayers
11. Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of influenza virus to perturb bilayers
12. Structural study of the interaction between the SIV fusion peptide and model membranes
13. Membrane fusion mediated by the influenza hemagglutinin requires the concerted action of at least three hemagglutinin trimers
14. Modulation of lipid polymorphism by the feline leukemia virus fusion peptide: Implications for the fusion mechanism
15. +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region
16. Lipid polymorphism and protein-lipid interactions
17. Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers
18. Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion
19. Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces
20. Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers
21. Structural studies on membrane-embedded influenza hemagglutinin and its fragments
22. pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers
23. Intrinsic curvature hypothesis for biomembrane lipid composition: A role for non-bilayer lipids
24. Stability of lyotropic phases with curved interfaces
25. Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: Probing the role of hydrophobic residue size in the central region of the fusion peptide
26. A host-guest system to study structure-function relationships of membrane fusion peptides
27. pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers
28. Molecular mechanisms and forces involved in the adhesion and fusion of amphiphilic bilayers
29. Effects of lipid packing on polymorphic phase behavior and membrane properties
30. Orientation of fusion-active synthetic peptides in phospholipid bilayers: Determination by Fourier transform infrared spectroscopy
31. Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion
32. A measure of helical propensity for amino acids in membrane environments
33. Interactions between neutral phospholipid bilayer membranes
34. Structure and topology of the influenza virus fusion peptide in lipid bilayers
35. The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR
36. 2-terminal HIV-1 gp41 peptide in fused and aggregated liposomes
37. Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer
38. The polar region consecutive to the HIV fusion peptide participates in membrane fusion
39. Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effects
40. Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution
41. Effect of nonpolar substitutions of the conserved Phe in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes
42. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
43. Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
44. Nucleated conformational conversion and the replication of conformational information by a prion determinant
45. Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms
46. The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: Implications for membrane fusion mechanisms
47. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion
48. Binding of apolipoprotein A-I model peptides to lipid bilayers
49. Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implication of α-helix formation for membrane fusion
50. Infrared spectroscopy of proteins and peptides in lipid bilayers
51. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
52. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin
53. Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
54. Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
55. Membrane protein folding and stability: Physical principles
56. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution