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Journal of Virology, February 2009, p. 1754-1766, Vol. 83, No. 4
0022-538X/09/$08.00+0     doi:10.1128/JVI.01855-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Rotavirus Architecture at Subnanometer Resolution {triangledown}

Zongli Li ,1,{dagger},{ddagger} Matthew L. Baker,1,{dagger} Wen Jiang,1,§ Mary K. Estes,3 and B. V. Venkataram Prasad2*

National Center for Macromolecular Imaging,1 Verna and Marrs Mclean Department of Biochemistry and Molecular Biology,2 Department of Molecular Virology and Microbiology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 770303

Received 3 September 2008/ Accepted 18 November 2008

Rotavirus, a nonturreted member of the Reoviridae, is the causative agent of severe infantile diarrhea. The double-stranded RNA genome encodes six structural proteins that make up the triple-layer particle. X-ray crystallography has elucidated the structure of one of these capsid proteins, VP6, and two domains from VP4, the spike protein. Complementing this work, electron cryomicroscopy (cryoEM) has provided relatively low-resolution structures for the triple-layer capsid in several biochemical states. However, a complete, high-resolution structural model of rotavirus remains unresolved. Combining new structural analysis techniques with the subnanometer-resolution cryoEM structure of rotavirus, we now provide a more detailed structural model for the major capsid proteins and their interactions within the triple-layer particle. Through a series of intersubunit interactions, the spike protein (VP4) adopts a dimeric appearance above the capsid surface, while forming a trimeric base anchored inside one of the three types of aqueous channels between VP7 and VP6 capsid layers. While the trimeric base suggests the presence of three VP4 molecules in one spike, only hints of the third molecule are observed above the capsid surface. Beyond their interactions with VP4, the interactions between VP6 and VP7 subunits could also be readily identified. In the innermost T=1 layer composed of VP2, visualization of the secondary structure elements allowed us to identify the polypeptide fold for VP2 and examine the complex network of interactions between this layer and the T=13 VP6 layer. This integrated structural approach has resulted in a relatively high-resolution structural model for the complete, infectious structure of rotavirus, as well as revealing the subtle nuances required for maintaining interactions in such a large macromolecular assembly.

* Corresponding author. Mailing address: Verna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Phone: (713) 798-5686. Fax: (713) 798-1625. E-mail: vprasad{at}bcm.tmc.edu

{triangledown} Published ahead of print on 26 November 2008.

{dagger} Co-first authors.

{ddagger} Present address: Harvard Medical School, Department of Cell Biology, Boston, MA 02115.

§ Present address: Markey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.

Journal of Virology, February 2009, p. 1754-1766, Vol. 83, No. 4
0022-538X/09/$08.00+0     doi:10.1128/JVI.01855-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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