A peptide pertaining to the loop segment of human immunodeficiency virus gp41 binds and interacts with model biomembranes: implications for the fusion mechanism.
The human immunodeficiency virus gp41 envelope protein mediates the entry of the virus into the target cell by promoting membrane fusion. In order to gain new insights into the viral fusion mechanism, we studied a 35-residue peptide pertaining to the loop domain of gp41, both in solution and membrane bound, by using infrared and fluorescence spectroscopy. We show here that the peptide, which has a membrane-interacting surface, binds and interacts with phospholipid model membranes and tends to aggregate in the presence of a membranous medium and induce the leakage of vesicle contents. The results reported in this work, i.e., the destabilization and fusion of negatively charged model membranes, suggest an essential role of the loop domain in the membrane fusion process induced by gp41.
Pascual
Roberto
R
Instituto de Biología Molecular y Celular, Universidad "Miguel Hernández," E-03202 Elche-Alicante, Spain.
Moreno
Miguel R
MR
Villalaín
José
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D005454:Fluorescence Polarization; D006678:HIV / Q000502:physiology*; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000378:metabolism*; D008561:Membrane Fusion / Q000502:physiology*; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010743:Phospholipids / Q000737:chemistry / Q000378:metabolism
D015700:HIV Envelope Protein gp41; D008563:Membrane Lipids; D010446:Peptide Fragments; D010743:Phospholipids