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Journal of Virology, March 2004, p. 2545-2552, Vol. 78, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.5.2545-2552.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Assembly Properties of the Human Immunodeficiency Virus Type 1 CA Protein

Barbie K. Ganser-Pornillos,1,{dagger} Uta K. von Schwedler,1 Kirsten M. Stray,1 Christopher Aiken,2 and Wesley I. Sundquist1*

Department of Biochemistry, University of Utah, Salt Lake City, Utah 84132,1 Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 372322

Received 5 February 2003/ Accepted 18 November 2003

During retroviral maturation, the CA protein oligomerizes to form a closed capsid that surrounds the viral genome. We have previously identified a series of deleterious surface mutations within human immunodeficiency virus type 1 (HIV-1) CA that alter infectivity, replication, and assembly in vivo. For this study, 27 recombinant CA proteins harboring 34 different mutations were tested for the ability to assemble into helical cylinders in vitro. These cylinders are composed of CA hexamers and are structural models for the mature viral capsid. Mutations that diminished CA assembly clustered within helices 1 and 2 in the N-terminal domain of CA and within the crystallographically defined dimer interface in the CA C-terminal domain. These mutations demonstrate the importance of these regions for CA cylinder production and, by analogy, mature capsid assembly. One CA mutant (R18A) assembled into cylinders, cones, and spheres. We suggest that these capsid shapes occur because the R18A mutation alters the frequency at which pentamers are incorporated into the hexagonal lattice. The fact that a single CA protein can simultaneously form all three known retroviral capsid morphologies supports the idea that these structures are organized on similar lattices and differ only in the distribution of 12 pentamers that allow them to close. In further support of this model, we demonstrate that the considerable morphological variation seen for conical HIV-1 capsids can be recapitulated in idealized capsid models by altering the distribution of pentamers.

* Corresponding author. Mailing address: Department of Biochemistry, University of Utah, 20 N 1900 E Rm. 211, Salt Lake City, UT 84132. Phone: (801) 585-5402. Fax: (801) 581-7959. E-mail: wes{at}biochem.utah.edu.

{dagger} Present address: Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037.

Journal of Virology, March 2004, p. 2545-2552, Vol. 78, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.5.2545-2552.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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