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Journal of Virology, January 2005, p. 1327-1332, Vol. 79, No. 2
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.2.1327-1332.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, Houston, Texas,1 Division of Infectious Diseases, School of Public Health, University of California, Berkeley, California,2 Department of Pediatrics,3 Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama4
Received 24 June 2004/ Accepted 23 August 2004
The smallest capsid proteins (SCPs) of the human herpesviruses differ substantially in size and sequence and are thought to impart some unique aspects of infection to their respective viruses. We used electron cryomicroscopy and antibody labeling to show that the 8-kDa SCP of human cytomegalovirus is attached only to major capsid protein subunits of the hexons, not the pentons. Thus, the SCPs of different herpesviruses illustrate that a protein can evolve significantly in sequence, structure, and function, while preserving its role in the architecture of the virus by binding to a specific partner in a specific oligomeric state.
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