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Biophysical Journal 84:2585-2592 (2003)
© 2003 The Biophysical Society

Penton Release from P22 Heat-Expanded Capsids Suggests Importance of Stabilizing Penton-Hexon Interactions during Capsid Maturation

Carolyn M. Teschke*, Amy McGough{dagger} and Pamela A. Thuman-Commike{ddagger}

* Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269; {dagger} Department of Biological Sciences and Markey Center for Structural Biology, Purdue University, West Lafayette, Indiana 47907; and {ddagger} QED Labs, San Jose, California 95128

Correspondence: Address reprint requests to Pamela A. Thuman-Commike, Tel.: 408-295-8347; Fax: 408-295-8348; E-mail: pam{at}qedlabs.com.

Bacteriophage assembly frequently begins with the formation of a precursor capsid that serves as a DNA packaging machine. The DNA packaging is accompanied by a morphogenesis of the small round precursor capsid into a large polyhedral DNA-containing mature phage. In vitro, this transformation can be induced by heat or chemical treatment of P22 procapsids. In this work, we examine bacteriophage P22 morphogenesis by comparing three-dimensional structures of capsids expanded both in vitro by heat treatment and in vivo by DNA packaging. The heat-expanded capsid reveals a structure that is virtually the same as the in vivo expanded capsid except that the pentons, normally present at the icosahedral fivefold positions, have been released. The similarities of these two capsid structures suggest that the mechanism of heat expansion is similar to in vivo expansion. The loss of the pentons further suggests the necessity of specific penton-hexon interactions during expansion. We propose a model whereby the penton-hexon interactions are stabilized through interactions of DNA, coat protein, and other minor proteins. When considered in the context of other studies using chemical or heat treatment of capsids, our study indicates that penton release may be a common trend among double-stranded DNA containing viruses.




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