The HIV-1 gp41 N-terminal heptad repeat plays an essential role in membrane fusion

Biochemistry
Kelly Sackett, Y Shai

Abstract

For many different enveloped viruses the crystal structure of the fusion protein core has been established. A striking conservation in the tertiary and quaternary arrangement of these core structures is repeatedly revealed among members of diverse families. It has been proposed that the primary role of the core involves structural rearrangements which facilitate apposition between viral and target cell membranes. Forming the internal trimeric coiled coil of the core, the N-terminal heptad repeat (NHR) of HIV-1 gp41 was suggested to have additional roles, due to its ability to bind biological membranes. The NHR is adjacent to the N-terminal hydrophobic fusion peptide (FP), which alone can fuse biological membranes. To investigate the role of the NHR in membrane fusion, we synthesized and functionally characterized HIV-1 gp41 peptides corresponding to the FP and NHR alone, as well as continuous peptides made of both FP and NHR (wild type and mutant). We show here that a consecutive, 70-residue peptide consisting of both the FP and NHR (gp41/1-70) has dramatic fusogenic properties. The effect of including the complete NHR, as compared to shorter 23-, 33-, or 52-residue N-terminal peptides, is illustrated by a leap in lipid mixing ...Continue Reading

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Citations

Nov 8, 2006·European Biophysics Journal : EBJ·Johannes ReichertAnne S Ulrich
Jan 29, 2011·European Biophysics Journal : EBJ·Dorit GrasnickAnne S Ulrich
Dec 4, 2003·Drug Discovery Today·Hiroyuki KamiyaHideyoshi Harashima
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Jul 26, 2015·The Biochemical Journal·Agnieszka Fedoruk-WyszomirskaJan Barciszewski
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Mar 22, 2020·Biochimica Et Biophysica Acta. Biomembranes·Christopher Aisenbrey, Burkhard Bechinger

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