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Journal of Virology, June 2008, p. 5951-5961, Vol. 82, No. 12
0022-538X/08/$08.00+0     doi:10.1128/JVI.00214-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Critical Role of Conserved Hydrophobic Residues within the Major Homology Region in Mature Retroviral Capsid Assembly {triangledown}

John G. Purdy,1 John M. Flanagan,2 Ira J. Ropson,2 Kristen E. Rennoll-Bankert,3,{dagger} and Rebecca C. Craven1*

Department of Microbiology and Immunology,1 Department of Biochemistry and Molecular Biology, The Pennsylvania State University, College of Medicine, Hershey, Pennsylvania 17033,2 Cedar Crest College, Allentown, Pennsylvania 181043

Received 30 January 2008/ Accepted 28 March 2008

During retroviral maturation, the CA protein undergoes dramatic structural changes and establishes unique intermolecular interfaces in the mature capsid shell that are different from those that existed in the immature precursor. The most conserved region of CA, the major homology region (MHR), has been implicated in both immature and mature assembly, although the precise contribution of the MHR residues to each event has been largely undefined. To test the roles of specific MHR residues in mature capsid assembly, an in vitro system was developed that allowed for the first-time formation of Rous sarcoma virus CA into structures resembling authentic capsids. The ability of CA to assemble organized structures was destroyed by substitutions of two conserved hydrophobic MHR residues and restored by second-site suppressors, demonstrating that these MHR residues are required for the proper assembly of mature capsids in addition to any role that these amino acids may play in immature particle assembly. The defect caused by the MHR mutations was identified as an early step in the capsid assembly process. The results provide strong evidence for a model in which the hydrophobic residues of the MHR control a conformational reorganization of CA that is needed to initiate capsid assembly and suggest that the formation of an interdomain interaction occurs early during maturation.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033. Phone: (717) 531-3528. Fax: (717) 531-6522. E-mail: rcraven{at}psu.edu

{triangledown} Published ahead of print on 9 April 2008.

{dagger} Present address: Department of Pathology, Johns Hopkins School of Medicine, Baltimore, MD 21205.

Journal of Virology, June 2008, p. 5951-5961, Vol. 82, No. 12
0022-538X/08/$08.00+0     doi:10.1128/JVI.00214-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Heslin, D. J., Murcia, P., Arnaud, F., Van Doorslaer, K., Palmarini, M., Lenz, J. (2009). A Single Amino Acid Substitution in a Segment of the CA Protein within Gag That Has Similarity to Human Immunodeficiency Virus Type 1 Blocks Infectivity of a Human Endogenous Retrovirus K Provirus in the Human Genome. J. Virol. 83: 1105-1114 [Abstract] [Full Text]  


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