@article {6335,
	title = {Atomic model of an infectious rotavirus particle.},
	journal = {The EMBO Journal},
	volume = {30},
	year = {2011},
	month = {2011 Jan 19},
	pages = {408-16},
	abstract = {<p>Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 {\r A} resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the β-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry.</p>
},
	keywords = {Capsid Proteins, Cell Membrane, Cryoelectron Microscopy, Crystallography, Models, Molecular, Protein Structure, Rotavirus, Secondary, Virion, Virus Internalization},
	issn = {1460-2075},
	doi = {10.1038/emboj.2010.322},
	author = {Settembre, Ethan C and Chen, James Z and Dormitzer, Philip R and Grigorieff, Nikolaus and Harrison, Stephen C}
}
@article {6342,
	title = {Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {106},
	year = {2009},
	month = {2009 Jun 30},
	pages = {10644-8},
	abstract = {<p>Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.</p>
},
	keywords = {Antigens, Biological, Calcium, Capsid Proteins, Cryoelectron Microscopy, Crystallography, Models, Molecular, Protein Multimerization, Protein Structure, Quaternary, Rotavirus, Viral, Viral Core Proteins, Virion, X-Ray},
	issn = {1091-6490},
	doi = {10.1073/pnas.0904024106},
	author = {Chen, James Z and Settembre, Ethan C and Aoki, Scott T and Zhang, Xing and Bellamy, A Richard and Dormitzer, Philip R and Harrison, Stephen C and Grigorieff, Nikolaus}
}
