scholarly journals 13C−13C Correlation Spectroscopy of Membrane-Associated Influenza Virus Fusion Peptide Strongly Supports a Helix-Turn-Helix Motif and Two Turn Conformations

2009 ◽  
Vol 131 (37) ◽  
pp. 13228-13229 ◽  
Author(s):  
Yan Sun ◽  
David P. Weliky
Keyword(s):  
Influenza Virus ◽  
Fusion Peptide ◽  
Correlation Spectroscopy ◽  
Virus Fusion

Design and function of a conformationally restricted analog of the influenza virus fusion peptide

2003 ◽  
Vol 62 (1) ◽  
pp. 19-26 ◽  
Author(s):  
A. Bertocco ◽  
F. Formaggio ◽  
C. Toniolo ◽  
Q.B. Broxterman ◽  
R.F. Epand ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Fusion Peptide ◽  
Conformationally Restricted ◽  
Virus Fusion ◽  
And Function

Interaction of Influenza Virus Fusion Peptide with Lipid Membranes: Effect of Lysolipid

2006 ◽  
Vol 211 (3) ◽  
pp. 191-200 ◽  
Author(s):  
S. Ohki ◽  
G.A. Baker ◽  
P.M. Page ◽  
T.A. McCarty ◽  
R.M. Epand ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Lipid Membranes ◽  
Fusion Peptide ◽  
Virus Fusion

scholarly journals 15N NMR Study of the Ionization Properties of the Influenza Virus Fusion Peptide in Zwitterionic Phospholipid Dispersions

2000 ◽  
Vol 78 (5) ◽  
pp. 2418-2425 ◽  
Author(s):  
Zhe Zhou ◽  
Jed C. Macosko ◽  
Donald W. Hughes ◽  
Brian G. Sayer ◽  
John Hawes ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Fusion Peptide ◽  
15N Nmr ◽  
Virus Fusion ◽  
Nmr Study

scholarly journals Structure and Topology of the Influenza Virus Fusion Peptide in Lipid Bilayers

1995 ◽  
Vol 270 (46) ◽  
pp. 27606-27614 ◽  
Author(s):  
Jürgen Lüneberg ◽  
Isabelle Martin ◽  
Frank Nüßler ◽  
Jean-Marie Ruysschaert ◽  
Andreas Herrmann
Keyword(s):  
Influenza Virus ◽  
Lipid Bilayers ◽  
Fusion Peptide ◽  
And Topology ◽  
Virus Fusion

scholarly journals Role of Hemagglutinin Surface Density in the Initial Stages of Influenza Virus Fusion: Lack of Evidence for Cooperativity

2000 ◽  
Vol 74 (6) ◽  
pp. 2714-2720 ◽  
Author(s):  
Susanne Günther-Ausborn ◽  
Pieter Schoen ◽  
Ingrid Bartoldus ◽  
Jan Wilschut ◽  
Toon Stegmann
Keyword(s):  
Influenza Virus ◽  
Surface Density ◽  
Initial Rate ◽  
Fusion Activity ◽  
Cooperative Action ◽  
Lipid Ratio ◽  
Virus Fusion ◽  
Influenza Virus Hemagglutinin ◽  
Optimal Fusion

ABSTRACT Membrane fusion mediated by influenza virus hemagglutinin (HA) is believed to proceed via the cooperative action of multiple HA trimers. To determine the minimal number of HA trimers required to trigger fusion, and to assess the importance of cooperativity between these HA trimers, we have generated virosomes containing coreconstituted HAs derived from two strains of virus with different pH dependencies for fusion, X-47 (optimal fusion at pH 5.1; threshold at pH 5.6) and A/Shangdong (optimal fusion at pH 5.6; threshold at pH 6.0), and measured fusion of these virosomes with erythrocyte ghosts by a fluorescence lipid mixing assay. Virosomes with different X-47-to-A/Shangdong HA ratios, at a constant HA-to-lipid ratio, showed comparable ghost-binding activities, and the low-pH-induced conformational change of A/Shangdong HA did not affect the fusion activity of X-47 HA. The initial rate of fusion of these virosomes at pH 5.7 increased directly proportional to the surface density of A/Shangdong HA, and a single A/Shangdong trimer per virosome appeared to suffice to induce fusion. The reciprocal of the lag time before the onset of fusion was directly proportional to the surface density of fusion-competent HA. These results support the notion that there is no cooperativity between HA trimers during influenza virus fusion.

Estimation by radiation inactivation of the size of functional units governing Sendai and influenza virus fusion

Biochemistry ◽  
1987 ◽  
Vol 26 (19) ◽  
pp. 6223-6227 ◽  
Author(s):  
Keiko Bundo-Morita ◽  
Suzanne Gibson ◽  
John Lenard
Keyword(s):  
Influenza Virus ◽  
Radiation Inactivation ◽  
Virus Fusion ◽  
Functional Units

scholarly journals New Insights into the Spring-Loaded Conformational Change of Influenza Virus Hemagglutinin

2002 ◽  
Vol 76 (9) ◽  
pp. 4456-4466 ◽  
Author(s):  
Jennifer A. Gruenke ◽  
R. Todd Armstrong ◽  
William W. Newcomb ◽  
Jay C. Brown ◽  
Judith M. White
Keyword(s):  
Influenza Virus ◽  
Conformational Change ◽  
Conformational Changes ◽  
Limited Proteolysis ◽  
Coiled Coil ◽  
Fusion Peptide ◽  
Wild Type ◽  
Influenza Virus Hemagglutinin ◽  
Target Membrane ◽  
Mutant Forms

ABSTRACT Influenza virus hemagglutinin undergoes a conformational change in which a loop-to-helix “spring-loaded” conformational change forms a coiled coil that positions the fusion peptide for interaction with the target bilayer. Previous work has shown that two proline mutations designed to disrupt this change disrupt fusion but did not determine the basis for the fusion defect. In this work, we made six additional mutants with single proline substitutions in the region that undergoes the spring-loaded conformational change and two additional mutants with double proline substitutions in this region. All double mutants were fusion inactive. We analyzed one double mutant, F63P/F70P, as an example. We observed that F63P/F70P undergoes key low-pH-induced conformational changes and binds tightly to target membranes. However, limited proteolysis and electron microscopy observations showed that the mutant forms a coiled coil that is only ∼50% the length of the wild type, suggesting that it is splayed in its N-terminal half. This work further supports the hypothesis that the spring-loaded conformational change is necessary for fusion. Our data also indicate that the spring-loaded conformational change has another role beyond presenting the fusion peptide to the target membrane.

scholarly journals Structural Characterizations of Fusion Peptide Analogs of Influenza Virus Hemagglutinin

2002 ◽  
Vol 277 (25) ◽  
pp. 22725-22733 ◽  
Author(s):  
Chun-Hua Hsu ◽  
Shih-Hsiung Wu ◽  
Ding-Kwo Chang ◽  
Chinpan Chen
Keyword(s):  
Influenza Virus ◽  
Fusion Peptide ◽  
Peptide Analogs ◽  
Influenza Virus Hemagglutinin ◽  
Structural Characterizations
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