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Originally published In Press as doi:10.1074/jbc.M910145199 on March 9, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16037-16043, May 26, 2000
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Virus Maturation Targets the Protein Capsid to Concerted Disassembly and Unfolding*

Andréa C. OliveiraDagger §, Andre M. O. GomesDagger §, Fábio C. L. AlmeidaDagger , Ronaldo Mohana-BorgesDagger , Ana Paula ValenteDagger , Vijay S. Reddy, John E. Johnson, and Jerson L. SilvaDagger ||

From the Dagger  Departamento de Bioquímica Médica, Instituto de Ciências Biomédicas, Centro Nacional de Ressonância Magnética Nuclear de Macromoléculas, Universidade Federal do Rio de Janeiro, 21941-590 Rio de Janeiro, RJ, Brazil and the  Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037

Many animal viruses undergo post-assembly proteolytic cleavage that is required for infectivity. The role of maturation cleavage on Flock House virus was evaluated by comparing wild type (wt) and cleavage-defective mutant (D75N) Flock House virus virus-like particles. A concerted dissociation and unfolding of the mature wt particle was observed under treatment by urea, whereas the cleavage-defective mutant dissociated to folded subunits as determined by steady-state and dynamic fluorescence spectroscopy, circular dichroism, and nuclear magnetic resonance. The folded D75N alpha  subunit could reassemble into capsids, whereas the yield of reassembly from unfolded cleaved wt subunits was very low. Overall, our results demonstrate that the maturation/cleavage process targets the particle for an "off pathway" disassembly, because dissociation is coupled to unfolding. The increased motions in the cleaved capsid, revealed by fluorescence and NMR, and the concerted nature of dissociation/unfolding may be crucial to make the mature particle infectious.

* This work was supported in part by an International Grant from the Howard Hughes Medical Institute (to J. L. S.) and by grants from Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Financiadora de Estudos e Projetos and Programa de Núcleos de Excelência of Brazil (to J. L. S.), and by a grant from the National Institutes of Health (to J. E. J.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

|| Howard Hughes Medical Institute International Scholar. To whom correspondence should be addressed. Tel.: 5521-590-4548; Fax: 5521-270-8647; E-mail: jerson@bioqmed.ufrj.br.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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