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Journal of Virology, June 2003, p. 6332-6340, Vol. 77, No. 11
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.11.6332-6340.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Structure of Intracellular Mature Vaccinia Virus Visualized by In Situ Atomic Force Microscopy

A. J. Malkin,1,2* A. McPherson,2 and P. D. Gershon3

BioSecurity and NanoSciences Laboratory, Department of Chemistry and Materials Science, Lawrence Livermore National Laboratory, Livermore, California 94551,1 Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900,2 Department of Medical Biochemistry and Genetics, Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, Texas 770303

Received 14 November 2002/ Accepted 4 March 2003

Vaccinia virus, the basis of the smallpox vaccine, is one of the largest viruses to replicate in humans. We have used in situ atomic force microscopy (AFM) to directly visualize fully hydrated, intact intracellular mature vaccinia virus (IMV) virions and chemical and enzymatic treatment products thereof. The latter included virion cores, core-enveloping coats, and core substructures. The isolated coats appeared to be composed of a highly cross-linked protein array. AFM imaging of core substructures indicated association of the linear viral DNA genome with a segmented protein sheath forming an extended ~16-nm-diameter filament with helical surface topography; enclosure of this filament within a 30- to 40-nm-diameter tubule which also shows helical topography; and enclosure of the folded, condensed 30- to 40-nm-diameter tubule within the core by a wall covered with peg-like projections. Proteins observed attached to the 30- to 40-nm-diameter tubules may mediate folding and/or compaction of the tubules and/or represent vestiges of the core wall and/or pegs. An accessory "satellite domain" was observed protruding from the intact core. This corresponded in size to isolated 70- to 100-nm-diameter particles that were imaged independently and might represent detached accessory domains. AFM imaging of intact virions indicated that IMV underwent a reversible shrinkage upon dehydration (as much as 2.2- to 2.5-fold in the height dimension), accompanied by topological and topographical changes, including protrusion of the satellite domain. As shown here, the chemical and enzymatic dissection of large, asymmetrical virus particles in combination with in situ AFM provides an informative complement to other structure determination techniques.

* Corresponding author: Mailing address: Department of Chemistry and Materials Science, Lawrence Livermore National Laboratory, L-233, P.O. Box 808, Livermore, CA 94551. Phone: (925) 422-7903. Fax: (925) 422-2041. E-mail: malkin1{at}llnl.gov.

Journal of Virology, June 2003, p. 6332-6340, Vol. 77, No. 11
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.11.6332-6340.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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