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Published online
doi:10.1083/jcb.200705062
The Journal of Cell Biology, Vol. 179, No. 4, 627-633
The Rockefeller University Press, 0021-9525 $30.00
© Shnyrova et al.
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Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain



Anna V. Shnyrova1,2, Juan Ayllon2, Ilya I. Mikhalyov1, Enrique Villar2, Joshua Zimmerberg1, and Vadim A. Frolov1

1 Laboratory of Cellular and Molecular Biophysics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892
2 Departamento de Bioquímica y Biología Molecular, Universidad de Salamanca, Salamanca 37007, Spain

Correspondence to J. Zimmerberg: joshz{at}mail.nih.gov

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.

I.I. Mikhalyov's present address is Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

Abbreviations used in this paper: ANTS/DPX, 8-aminonaphthalene–1,3,6– trisulfonic acid/p-xylene-bis-pyridium bromide; BODIPY, boron dipyrromethane difluoride; DOPE, dioleoyl-PE; GUV, giant unilamellar vesicle; LUV, large unilamellar vesicle; M, matrix protein of NDV; NDV, Newcastle disease virus; PC, phosphocholine; PE, phosphoethanolamine; Rh, rhodamine.


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