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Journal of Virology, March 2003, p. 3418-3429, Vol. 77, No. 6
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.6.3418-3429.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Vaccinia Virus G7L Protein Interacts with the A30L Protein and Is Required for Association of Viral Membranes with Dense Viroplasm To Form Immature Virions

Patricia Szajner,1,2 Howard Jaffe,3 Andrea S. Weisberg,1 and Bernard Moss1*

Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,1 Protein/Peptide Sequence Facility, National Institute of Neurological Disorders and Stroke,3 National Institutes of Health, Bethesda, Maryland 20892, and Graduate Program of the Department of Genetics, The George Washington University, Washington, D.C. 200522

Received 18 October 2002/ Accepted 11 December 2002

The vaccinia virus A30L protein is required for the association of electron-dense, granular, proteinaceous material with the concave surfaces of crescent membranes, an early step in viral morphogenesis. For the identification of additional proteins involved in this process, we used an antibody to the A30L protein, or to an epitope appended to its C terminus, to capture complexes from infected cells. A prominent 42-kDa protein was resolved and identified by mass spectrometry as the vaccinia virus G7L protein. This previously uncharacterized protein was expressed late in infection and was associated with immature virions and the cores of mature particles. In order to study the role of the G7L protein, a conditional lethal mutant was made by replacing the G7L gene with an inducible copy. Expression of G7L and formation of infectious virus was dependent on the addition of inducer. Under nonpermissive conditions, morphogenesis was blocked and viral crescent membranes and immature virions containing tubular elements were separated from the electron-dense granular viroplasm, which accumulated in large spherical masses. This phenotype was identical to that previously obtained with an inducible, conditional lethal A30L mutant. Additional in vivo and in vitro experiments provided evidence for the direct interaction of the A30L and G7L proteins and demonstrated that the stability of each one was dependent on its association with the other.

* Corresponding author. Mailing address: Laboratory of Viral Diseases, National Institutes of Health, 4 Center Dr., MSC 0445, Bethesda, MD 20892-0445. Phone: (301) 496-9869. Fax: (301) 480-1147. E-mail: bmoss{at}nih.gov.

Journal of Virology, March 2003, p. 3418-3429, Vol. 77, No. 6
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.6.3418-3429.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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