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© The Rockefeller University Press, 0021-9525/1999//267 $5.00
The Journal of Cell Biology, Volume 144, Number 2, , 1999 267-279

An Unconventional Role for Cytoplasmic Disulfide Bonds in Vaccinia Virus Proteins

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.

Key Words: poxviridae • viral assembly • vaccinia virus • disulfide bonding • reducing agents

Abbreviations used in this paper: 2-D, two-dimensional; EEV, extracellular enveloped virus; GSH, reduced glutathione; GSSG, oxidized glutathione; HA, hemagglutinin; IC, intermediate compartment; IMV, intracellular mature virus; MOI, multiplicity of infection; PDI, protein disulfide isomerase; PFU, plaque-forming units; PNS, post-nuclear supernatant; vv, vaccinia virus.

Part of this work was supported by a Human Frontier Science Program fellowship to J. Krijnse Locker.

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