Structural Properties of gp41 Fusion Peptide at a Model Membrane Interface

2013 ◽  
Vol 117 (49) ◽  
pp. 15527-15535 ◽  
Author(s):  
V. Volkov ◽  
M. Bonn
1998 ◽  
Vol 95 (2) ◽  
pp. 467-473 ◽  
Author(s):  
A. Schanck ◽  
R. Brasseur ◽  
J. Peuvot

2015 ◽  
Vol 119 (18) ◽  
pp. 5846-5856 ◽  
Author(s):  
Krzysztof Murzyn ◽  
Marta Pasenkiewicz-Gierula

2017 ◽  
Vol 1861 (2) ◽  
pp. 97-105 ◽  
Author(s):  
Remigiusz Worch ◽  
Joanna Krupa ◽  
Alicja Filipek ◽  
Anna Szymaniec ◽  
Piotr Setny

2014 ◽  
Vol 106 (2) ◽  
pp. 53a
Author(s):  
Diana Lousa ◽  
Bruno L. Victor ◽  
Carlos Fernandez ◽  
Cláudio M. Soares

2000 ◽  
Vol 74 (17) ◽  
pp. 8038-8047 ◽  
Author(s):  
Tatiana Suárez ◽  
William R. Gallaher ◽  
Aitziber Agirre ◽  
Félix M. Goñi ◽  
José L. Nieva

ABSTRACT We have identified a region within the ectodomain of the fusogenic human immunodeficiency virus type 1 (HIV-1) gp41, different from the fusion peptide, that interacts strongly with membranes. This conserved sequence, which immediately precedes the transmembrane anchor, is not highly hydrophobic according to the Kyte-Doolittle hydropathy prediction algorithm, yet it shows a high tendency to partition into the membrane interface, as revealed by the Wimley-White interfacial hydrophobicity scale. We have investigated here the membrane effects induced by NH2-DKWASLWNWFNITNWLWYIK-CONH2(HIVc), the membrane interface-partitioning region at the C terminus of the gp41 ectodomain, in comparison to those caused by NH2-AVGIGALFLGFLGAAGSTMGARS-CONH2(HIVn), the fusion peptide at the N terminus of the subunit. Both HIVc and HIVn were seen to induce membrane fusion and permeabilization, although lower doses of HIVc were required for comparable effects to be detected. Experiments in which equimolar mixtures of HIVc and HIVn were used indicated that both peptides may act in a cooperative way. Peptide-membrane and peptide-peptide interactions underlying those effects were further confirmed by analyzing the changes in fluorescence of peptide Trp residues. Replacement of the first three Trp residues by Ala, known to render a defective gp41 phenotype unable to mediate both cell-cell fusion and virus entry, also abrogated the HIVc ability to induce membrane fusion or form complexes with HIVn but not its ability to associate with vesicles. Hydropathy analysis indicated that the presence of two membrane-partitioning stretches separated by a collapsible intervening sequence is a common structural motif among other viral envelope proteins. Moreover, sequences with membrane surface-residing residues preceding the transmembrane anchor appeared to be a common feature in viral fusion proteins of several virus families. According to our experimental results, such a feature might be related to their fusogenic function.


2015 ◽  
Vol 137 (32) ◽  
pp. 10190-10198 ◽  
Author(s):  
Bei Ding ◽  
Afra Panahi ◽  
Jia-Jung Ho ◽  
Jennifer E. Laaser ◽  
Charles L. Brooks ◽  
...  

1996 ◽  
Vol 118 (17) ◽  
pp. 4001-4008 ◽  
Author(s):  
Brian A. Salvatore ◽  
Ranajeet Ghose ◽  
James H. Prestegard

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