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Bacteriophage HK97 Capsid Assembly and Maturation

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 726))

Abstract

The Escherichia coli phage HK97 has provided a productive experimental system for investigating how virus capsids are assembled from their protein components and how the assembled capsids mature to their final form. Aspects of the process for which the HK97 system has been particularly informative include assembly of the icosahedral capsid shell from the component proteins, structure of the capsid subunits and of the entire capsid as it progresses through its maturation, and the mechanism of the covalent cross-linking that links the subunits together into viral chain mail. The structural dynamics of the maturation as well as the energetics that drives maturation forward are beginning to be understood.

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Acknowledgments

The work described here is the product of a multilaboratory collaboration involving not only the two authors of this chapter but also Alasdair Steven, Bob Duda, and James Conway, as well as numerous graduate and undergraduate students, postdocs, and technical staff from all of our labs. There have been many important contributions as well from colleagues not as directly associated with the central “HK97 Cabal,” including Lars Liljas, Philip Ross, George Thomas, Hiro Tsuruta, and their associates. Credit for our current understanding of HK97 capsid assembly and maturation is jointly owned. Work on this topic in the labs of the two authors of this chapter has been supported by NIH grants R01-GM47795 (RWH) and R01-AI40101 and R01-GM54076 (JEJ).

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Correspondence to Roger W. Hendrix .

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Hendrix, R.W., Johnson, J.E. (2012). Bacteriophage HK97 Capsid Assembly and Maturation. In: Rossmann, M., Rao, V. (eds) Viral Molecular Machines. Advances in Experimental Medicine and Biology, vol 726. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-0980-9_15

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