Por favor, use este identificador para citar o enlazar este ítem: http://hdl.handle.net/10259/8375
Título
Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain
Autor
Publicado en
The Journal of Cell Biology. 2007, V. 179, n. 4, p. 627-633
Editorial
Rockefeller University Press
Fecha de publicación
2007-11
ISSN
0021-9525
DOI
10.1083/jcb.200705062
Abstract
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.
Materia
Bioquímica
Biochemistry
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