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Journal of Virology, November 2004, p. 12668-12671, Vol. 78, No. 22
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.22.12668-12671.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Structure and Polymorphism of the UL6 Portal Protein of Herpes Simplex Virus Type 1

Benes L. Trus,1,2 Naiqian Cheng,2 William W. Newcomb,3 Fred L. Homa,4 Jay C. Brown,3 and Alasdair C. Steven2*

Imaging Sciences Laboratory, Division of Computational Bioscience, Center for Information Technology,1 Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland,2 Department of Microbiology and Cancer Center, University of Virginia Health System, Charlottesville, Virginia,3 Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania4

Received 10 May 2004/ Accepted 23 June 2004

By electron microscopy and image analysis, we find that baculovirus-expressed UL6 is polymorphic, consisting of rings of 11-, 12-, 13-, and 14-fold symmetry. The 12-mer is likely to be the oligomer incorporated into procapsids: at a resolution of 16 Å, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins.

* Corresponding author. Mailing address: Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Building 50, Room 1517, MSC 8025, 50 South Dr., Bethesda, MD 20892-8025. Phone: (301) 496-0132. Fax: (301) 443-7651. E-mail: Alasdair_Steven{at}nih.gov.

Journal of Virology, November 2004, p. 12668-12671, Vol. 78, No. 22
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.22.12668-12671.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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