Deacylation of influenza virus hemagglutinin does not affect the kinetics of low pH induced membrane fusion

1996 ◽  
Vol 431 (S6) ◽  
pp. R257-R258 ◽  
Author(s):  
Britta Schroth ◽  
Hans C. Philipp ◽  
Michael Veit ◽  
Michael F. G. Schmidt ◽  
Andreas Herrmann
Keyword(s):  
Influenza Virus ◽  
Membrane Fusion ◽  
Low Ph ◽  
Induced Membrane ◽  
Influenza Virus Hemagglutinin ◽  
Kinetics Of

scholarly journals Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin.

1987 ◽  
Vol 105 (6) ◽  
pp. 2887-2896 ◽  
Author(s):  
J M White ◽  
I A Wilson
Keyword(s):  
Influenza Virus ◽  
Membrane Fusion ◽  
Conformational Change ◽  
Conformational Changes ◽  
Three Dimensional ◽  
Low Ph ◽  
Protein Conformational Changes ◽  
Influenza Virus Hemagglutinin ◽  
Protein Conformational Change ◽  
Peptide Antibodies

At low pH, the hemagglutinin (HA) of influenza virus undergoes an irreversible conformational change that potentiates its essential membrane fusion function. We have probed the details of this conformational change using a panel of 14 anti-HA-peptide antibodies. Whereas some antibodies reacted equally well with both the neutral and low-pH HA conformations, others reacted to a significantly greater extent with the low-pH form. The locations of the peptides recognized by the latter antibodies in the three-dimensional HA structure indicated regions of the protein that change in response to low pH. Moreover, kinetic experiments suggested steps in the conformational change. In addition to their relevance to membrane fusion, our results show that anti-peptide antibodies can be used to study some types of biologically important protein conformational changes.

An ultrastructural approach to influenza virus hemagglutinin-induced membrane fusion

1989 ◽  
Vol 31 (4) ◽  
pp. 460
Author(s):  
KoertN.J. Burger ◽  
Gerhard Knoll ◽  
Gerrit van Meer ◽  
ArieJ. Verkleij
Keyword(s):  
Influenza Virus ◽  
Membrane Fusion ◽  
Induced Membrane ◽  
Influenza Virus Hemagglutinin

scholarly journals A Functional F Analogue of Autographa californica Nucleopolyhedrovirus GP64 from the Agrotis segetum Granulovirus

2008 ◽  
Vol 82 (17) ◽  
pp. 8922-8926 ◽  
Author(s):  
Feifei Yin ◽  
Manli Wang ◽  
Ying Tan ◽  
Fei Deng ◽  
Just M. Vlak ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Plutella Xylostella ◽  
Syncytium Formation ◽  
Low Ph ◽  
Autographa Californica ◽  
Agrotis Segetum ◽  
Induced Membrane ◽  
F Protein ◽  
Autographa Californica Nucleopolyhedrovirus

ABSTRACT The envelope fusion protein F of Plutella xylostella granulovirus is a computational analogue of the GP64 envelope fusion protein of Autographa californica nucleopolyhedrovirus (AcMNPV). Granulovirus (GV) F proteins were thought to be unable to functionally replace GP64 in the AcMNPV pseudotyping system. In the present study the F protein of Agrotis segetum GV (AgseGV) was identified experimentally as the first functional GP64 analogue from GVs. AgseF can rescue virion propagation and infectivity of gp64-null AcMNPV. The AgseF-pseudotyped AcMNPV also induced syncytium formation as a consequence of low-pH-induced membrane fusion.

scholarly journals Structural Insights into the Membrane Fusion Mechanism Mediated by Influenza Virus Hemagglutinin

Biochemistry ◽  
2014 ◽  
Vol 53 (5) ◽  
pp. 846-854 ◽  
Author(s):  
Fengyun Ni ◽  
Xiaorui Chen ◽  
Jun Shen ◽  
Qinghua Wang
Keyword(s):  
Influenza Virus ◽  
Membrane Fusion ◽  
Influenza Virus Hemagglutinin ◽  
Structural Insights
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