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Journal of Virology, February 2003, p. 2730-2735, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2730-2735.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Interaction between the Major Capsid Protein and the Smallest Capsid Protein of Human Cytomegalovirus Is Dependent on Two Linear Sequences in the Smallest Capsid Protein

Lilin Lai1 and William J. Britt2,3*

Departments of Medicine,1 Pediatrics,2 Microbiology, University of Alabama at Birmingham, Birmingham, Alabama3

Received 18 June 2002/ Accepted 4 October 2002

The assembly of human cytomegalovirus (HCMV) with recombinant systems has not been accomplished. An understanding of specific interactions between individual capsid proteins could point to unique characteristics of the assembly process of HCMV capsids. Similar to its herpes simplex virus counterpart, VP26 (UL35), the HCMV smallest capsid protein (SCP; UL48/49) decorates hexons in the mature capsid. In contrast to VP26, the HCMV SCP is essential for virus assembly. In this study we have shown that the major capsid protein (MCP) and the SCP interact in the cytoplasm of transfected cells and can be coprecipitated from insect cells expressing the MCP and the SCP. Using a two-hybrid reporter assay, we demonstrated that two linear sequences within the SCP are sufficient for SCP and MCP interactions.

* Corresponding author. Mailing address: Department of Pediatrics, Room 733, 1600 7th Ave. South, Birmingham, AL 35233. Phone: (205) 939-9590. Fax: (205) 975-6549. E-mail: wbritt{at}peds.uab.edu.

Journal of Virology, February 2003, p. 2730-2735, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2730-2735.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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