title: Cholesterol mediates membrane curvature during fusion events.
abstract: Biomembranes undergo extensive shape changes as they perform vital cellular functions. The mechanisms by which lipids and proteins control membrane curvature remain unclear. We use x-ray reflectivity, grazing incidence x-ray diffraction, and epifluorescence microscopy to study binding of HIV-1 glycoprotein gp41's membrane-bending domain to DPPC/cholesterol monolayers of various compositions at the air-liquid interface. The results offer a new insight into how membrane curvature could be regulated by cholesterol during fusion of the viral lipid envelope and the host cell membranes.
authors.affiliation: Department of Physics and Center for Molecular Study of Condensed Soft Matter (μCoSM), Illinois Institute of Technology, Chicago, Illinois 60616, USA.
authors.forename: Andrey
authors.initials: A
authors.lastname: Ivankin
authors.forename: Ivan
authors.initials: I
authors.lastname: Kuzmenko
authors.forename: David
authors.initials: D
authors.lastname: Gidalevitz
mesh_terms: D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D002784:Cholesterol / Q000737:chemistry* / Q000378:metabolism; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000378:metabolism; D008561:Membrane Fusion; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D014961:X-Ray Diffraction
chemical_list: D015700:HIV Envelope Protein gp41; D008563:Membrane Lipids; D008565:Membrane Proteins; C514787:gp41 protein, Human immunodeficiency virus 1; D015060:1,2-Dipalmitoylphosphatidylcholine; D002784:Cholesterol