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Title: Architecture of a dsDNA viral capsid in complex with its maturation protease
Authors: Veesler, D.
Khayat, R.
Krishnamurthy, S.
Snijder, J.
Huang, R.K.
Heck, A.J.R.
Anand, G.S. 
Johnson, J.E.
Issue Date: 4-Feb-2014
Citation: Veesler, D., Khayat, R., Krishnamurthy, S., Snijder, J., Huang, R.K., Heck, A.J.R., Anand, G.S., Johnson, J.E. (2014-02-04). Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure 22 (2) : 230-237. ScholarBank@NUS Repository.
Abstract: Most double-stranded DNA (dsDNA) viruses, including bacteriophages and herpesviruses, rely on a staged assembly process of capsid formation. A viral protease is required for many of them to disconnect scaffolding domains/proteins from the capsid shell, therefore priming the maturation process. We used the bacteriophage HK97 as a model system to decipher the molecular mechanisms underlying the recruitment of the maturation protease by the assembling procapsid and the influence exerted onto the latter. Comparisons of the procapsid with and without protease using single-particle cryoelectron microscopy reconstructions, hydrogen/deuterium exchange coupled to mass spectrometry, and native mass spectrometry demonstrated that the protease interacts with the scaffolding domains within the procapsid interior and stabilizes them as well as the whole particle. The results suggest that the thermodynamic consequences of protease packaging are to shift the equilibrium between isolated coat subunit capsomers and procapsid in favor of the latter by stabilizing the assembled particle before making the process irreversible through proteolysis of the scaffolding domains. © 2014 Elsevier Ltd.
Source Title: Structure
ISSN: 09692126
DOI: 10.1016/j.str.2013.11.007
Appears in Collections:Staff Publications

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