RT info:eu-repo/semantics/article
T1 Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain
A1 Shnyrova, Anna V.
A1 Ayllón Barasoain, Juan
A1 Mikhalyov, Ilya I.
A1 Villar, Enrique
A1 Zimmerberg, Joshua
A1 Frolov, Vadim A.
K1 Bioquímica
K1 Biochemistry
AB The shape of enveloped viruses depends critically on an internal protein matrix, yet it remains unclear how the matrix proteins control the geometry of the envelope membrane. We found that matrix proteins purified from Newcastle disease virus adsorb on a phospholipid bilayer and condense into fluidlike domains that cause membrane deformation and budding of spherical vesicles, as seen by fluorescent and electron microscopy. Measurements of the electrical admittance of the membrane resolved the gradual growth and rapid closure of a bud followed by its separation to form a free vesicle. The vesicle size distribution, confined by intrinsic curvature of budding domains, but broadened by their merger, matched the virus size distribution. Thus, matrix proteins implement domain-driven mechanism of budding, which suffices to control the shape of these proteolipid vesicles.
PB Rockefeller University Press
SN 0021-9525
YR 2007
FD 2007-11
LK http://hdl.handle.net/10259/8375
UL http://hdl.handle.net/10259/8375
LA eng
NO Supported by the intramural research program of the National Institute of Child Health and Human Development; Spanish Fondo de Investigaciones Sanitarias grant FIS-PI051796, cofinanced by Fonds Européen de Développement Régional-Fonds Social Européen; and the Spanish Ministerio de Educación y Ciencia Formacíon de Profesorado Universitario program (predoctoral fellowship AP-2004-6065 to J. Ayllon).
DS Repositorio Institucional de la Universidad de Burgos
RD 12-may-2024