scholarly journals Acid-Induced Membrane Fusion by the Hemagglutinin Protein and Its Role in Influenza Virus Biology

Author(s):  
Charles J. Russell
1996 ◽  
Vol 431 (S6) ◽  
pp. R257-R258 ◽  
Author(s):  
Britta Schroth ◽  
Hans C. Philipp ◽  
Michael Veit ◽  
Michael F. G. Schmidt ◽  
Andreas Herrmann

1992 ◽  
Vol 267 (28) ◽  
pp. 20225-20232
Author(s):  
M Tsurudome ◽  
R Glück ◽  
R Graf ◽  
R Falchetto ◽  
U Schaller ◽  
...  

1997 ◽  
Vol 137 (5) ◽  
pp. 1041-1056 ◽  
Author(s):  
Toku Kanaseki ◽  
Kazunori Kawasaki ◽  
Masayuki Murata ◽  
Yoko Ikeuchi ◽  
Shun-ichi Ohnishi

The structure of membrane fusion intermediates between the A/PR/8(H1N1) strain of influenza virus and a liposome composed of egg phosphatidylcholine, cholesterol, and glycophorin was studied using quick-freezing electron microscopy. Fusion by viral hemagglutinin protein was induced at pH 5.0 and 23°C. After a 19-s incubation under these conditions, small protrusions with a diameter of 10–20 nm were found on the fractured convex faces of the liposomal membranes, and small pits complementary to the protrusions were found on the concave faces. The protrusions and pits corresponded to fractured parts of outward bendings of the lipid bilayer or “microprotrusions of the lipid bilayer.” At the loci of the protrusions and pits, liposomal membranes had local contacts with viral membranes. In many cases both the protrusions and the pits were aligned in regular polygonal arrangements, which were thought to reflect the array of hemagglutinin spikes on the viral surface. These structures were induced only when the medium was acidic with the virus present. Based on these observations, it was concluded that the microprotrusions of the lipid bilayer are induced by hemagglutinin protein. Furthermore, morphological evidence for the formation of the “initial fusion pore” at the microprotrusion was obtained. The protrusion on the convex face sometimes had a tiny hole with a diameter of <4 nm in the center. The pits transformed into narrow membrane connections <10 nm in width, bridging viruses and liposomes. The structures of the fusion pore and fusion neck with larger sizes were also observed, indicating growth of the protrusions and pits to distinct fusion sites. We propose that the microprotrusion of the lipid bilayer is a fusion intermediate induced by hemagglutinin protein, and suggest that the extraordinarily high curvature of this membrane structure is a clue to the onset of fusion. The possible architecture of the fusion intermediate is discussed with regard to the localization of intramembrane particles at the microprotrusion.


Biochemistry ◽  
1995 ◽  
Vol 34 (17) ◽  
pp. 5705-5711 ◽  
Author(s):  
Simon Nebel ◽  
Ingrid Bartoldus ◽  
Toon Stegmann

2012 ◽  
Vol 102 (3) ◽  
pp. 604a
Author(s):  
Caroline Mair ◽  
P. Sivaramakrishna Rachakonda ◽  
Thomas Korte ◽  
Andreas Herrmann

1989 ◽  
Vol 31 (4) ◽  
pp. 460
Author(s):  
KoertN.J. Burger ◽  
Gerhard Knoll ◽  
Gerrit van Meer ◽  
ArieJ. Verkleij

1994 ◽  
Vol 75 (2) ◽  
pp. 395-399 ◽  
Author(s):  
C. C. Pak ◽  
M. Krumbiegel ◽  
R. Blumenthal

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