2026-06-18T03:21:58Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/83752024-01-18T01:05:20Zcom_10259_4862com_10259_5086com_10259_2604col_10259_4863

Shnyrova, Anna V. Ayllón Barasoain, Juan Mikhalyov, Ilya I. Villar, Enrique Zimmerberg, Joshua Frolov, Vadim A. 2024-01-17T12:40:53Z 2024-01-17T12:40:53Z 2007-11 0021-9525 http://hdl.handle.net/10259/8375 10.1083/jcb.200705062 1540-8140 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. eng info:eu-repo/semantics/openAccess Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain info:eu-repo/semantics/article