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J. Cell Biol.,
Volume 144, Number 2, January 25, 1999 267-279
European Molecular Biology Laboratory, Cell Biology Programme, 69117 Heidelberg, Germany
Previous data have shown that reducing
agents disrupt the structure of vaccinia virus (vv). Here,
we have analyzed the disulfide bonding of vv proteins
in detail. In vv-infected cells cytoplasmically synthesized vv core proteins became disulfide bonded in the
newly assembled intracellular mature viruses (IMVs).
vv membrane proteins also assembled disulfide bonds,
but independent of IMV formation and to a large extent on their cytoplasmic domains. If disulfide bonding
was prevented, virus assembly was only partially impaired as shown by electron microscopy as well as a
biochemical assay of IMV formation. Under these conditions, however, the membranes around the isolated
particles appeared less stable and detached from the
underlying core. During the viral infection process
the membrane proteins remained disulfide bonded,
whereas the core proteins were reduced, concomitant
with delivery of the cores into the cytoplasm. Our data
show that vv has evolved an unique system for the assembly of cytoplasmic disulfide bonds that are localized
both on the exterior and interior parts of the IMV.
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