Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers

Virology

Volumn 297, Issue 1, 2002, Pages 128-135

  Roche, Stéphane ^a   Gaudin, Yves ^a  

^a CNRS   (France)

Author keywords

Conformational change; Glycoprotein; Membrane fusion; Rabies virus; Rhabdovirus

Indexed keywords

VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HYDROPHOBICITY; INCUBATION TIME; MEMBRANE FUSION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTON TRANSPORT; RABIES VIRUS; THERMODYNAMICS;

RABIES VIRUS; RHABDOVIRIDAE;

EID: 0036309399     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2002.1429     Document Type: Article

References (37)

1. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
2. Influenza hemagglutinin is spring-loaded by a metastable native conformation
3. The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
4. Gating kinetics of pH-activated membrane fusion of vesicular stomatitis virus with cells: Stopped-flow measurements by dequenching of octadecylrhodamine fluorescence
5. The meaning of Scatchard and Hill plots
6. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
7. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
8. Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses
9. Mechanisms of rabies virus neutralization
10. Rabies virus-induced membrane fusion pathway
11. Reversibility in fusion protein conformational changes. The intriguing case of rhabdovirus-induced membrane fusion
12. Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein
13. Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion
14. Rabies virus glycoprotein is a trimer
15. Reversible conformational changes and fusion activity of rabies virus glycoprotein
16. Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy
17. Secretory and viral fusion may share mechanistic events with fusion between curved lipid bilayers
18. Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusion
19. The fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
20. A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion
21. Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates
22. 125I]iodonaphthyl azide photolabeling studies in biological membranes
23. The initial fusion pore induced by baculovirus GP64 is large and forms quickly
24. Antigenic site II of the rabies virus glycoprotein: Structure and role in viral virulence
25. Role of viral envelope sialic acid in membrane fusion mediated by the vesicular stomatitis virus envelope glycoprotein
26. Monoclonal antibodies which recognize the acidic configuration of the rabies glycoprotein at the surface of the virion can be neutralizing
27. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
28. Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes
29. Mutations in a carboxy-terminal region of vesicular stomatitis virus glycoprotein G that affect membrane fusion activity
30. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion
31. Coiled coils in both intracellular vesicle and viral membrane fusion
32. Use of resonance energy transfer to monitor membrane fusion
33. Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virus-induced membrane fusion
34. Evidence for H(+)-induced insertion of influenza hemagglutinin HA2 N-terminal segment into viral membrane
35. Membrane fusion proteins of enveloped animal viruses
36. Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
37. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein