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Trehalose plays a new role in nanotechnology and research of cell walls
Trehalose plays a new role in nanotechnology and research of cell walls.

Comments by J. C. Spencer

Trehalose plays a new role in nanotechnology and the research of cell walls. The study of the capsid, the protein shell of a virus, will show us how to better protect ourselves from viruses. Structural analyses of capsid protein is the means to categorize viruses into families. Collaborative work around the world is helping our understanding of the cell and viruses. Rice University Houston has just pinpointed AND MADE X-RAY IMAGES of the five million atoms in the viral coat used by hundreds of viruses. This picture is worth a thousand words.

The report today is from two published works: Rice University and the role trehalose is playing in the research at other institutes.

Click here for the full report (pdf file).

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Image pinpoints all 5 million atoms in viral coat

Researchers decipher protective shield used by hundreds of viruses

Image 1

HOUSTON -- (Feb. 16, 2009) -- If a picture is worth a thousand words, then Rice University's precise new image of a virus' protective coat is seriously undervalued. More than three years in the making, the image contains some 5 million atoms -- each in precisely the right place -- and it could help scientists find better ways to both fight viral infections and design new gene therapies.

The stunning image, which appears online this week in the Proceedings of the National Academy of Sciences, reveals the structure of a type of protein coat shared by hundreds of known viruses containing double-stranded RNA genomes. The image was painstakingly created from hundreds of high-energy X-ray diffraction images and paints the clearest picture yet of the viruses' genome-encasing shell called a "capsid."

"When these viruses invade cells, the capsids get taken inside and never completely break apart," said lead researcher Jane Tao, assistant professor of biochemistry and cell biology at Rice.

Capsids come into play because viruses can reproduce themselves only by invading a host cell and highjacking its biochemical machinery. But when they invade, viruses need to seal off their genetic payload to prevent it from being destroyed by the cell's protective mechanisms.

Though there are more than 5,000 known viruses, including whole families that are marked by wide variations in genetic payload and other characteristics, most of them use either a helical or a spherical capsid.

In their attempt to map precisely the spherical variety, Tao and lead author Junhua Pan, a postdoctoral fellow at Rice, first had to create a crystalline form of the capsid that could be X-rayed. They chose the oft-studied Penicillium stoloniferum virus F, or PsV-F, a virus that infects the fungus that makes penicillin. PsV-F uses the spherical capsid; although it does not infect humans, it is similar to a rotavirus and others that do.

"Spherical viruses like this have symmetry like a soccer ball or geodesic dome," Pan said. "The whole capsid contains exactly 120 copies of a single protein."

Previous studies had shown that spherical capsids contain dozens of copies of the capsid protein, or CP, in an interlocking arrangement. The new research identified the sphere's basic building block, a four-piece arrangement of CP molecules called a tetramer, which could also be building blocks for other viruses' protein coats. By deciphering both the arrangement and the basic building block, the research team hopes to learn more about the capsid-forming process.

"Because many viruses use this type of capsid, understanding how it forms could lead to new approaches for antiviral therapies," Tao said. "It could also aid researchers who are trying to create designer viruses and other tools that can deliver therapeutic genes into cells."

The research team used X-ray crystallography to decipher the structure of the capsid. Pan first spent several months creating hundreds of crystal samples of PsV-F. He then collected hundreds of high-intensity, high-energy X-ray diffraction images at the Cornell High Energy Synchotron Source, or CHESS, in Ithaca, N.Y. By analyzing the way the X-rays scattered when they struck the crystals, Pan and the team created a precise three-dimensional image of the spherical capsid.

###

The research team included Rice postdoctoral researcher Li Lin and former graduate student Liping Dong; Max Nibert of Harvard Medical School; Timothy Baker, Wendy Ochoa and Robert Sinkovits, all of the University of California, San Diego; and Said Ghabrial and Wendy Havens, both of the University of Kentucky.

The research was supported by the National Institutes of Health, the USDA, the Welch Foundation, the Kresge Science Initiative Endowment Fund, the Agouron Foundation and the San Diego Supercomputer Center.

Contact: Jade Boyd
jadeboyd@rice.edu
713-348-6778
Rice University

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Long term storage of virus templated fluorescent materials for sensing applications

Abstract. Wild type, mutant, and chemically modified Cowpea mosaic viruses (CPMV) were studied for long term preservation in the presence and absence of cryoprotectants. Viral complexes were reconstituted and tested via fluorescence spectroscopy and a UV/vis-based RNase assay for structural integrity. When viruses lyophilized in the absence of cryoprotectant were rehydrated and RNase treated, UV absorption increased, indicating that the capsids were damaged. The addition of trehalose during lyophilization protected capsid integrity for at least 7 weeks. Measurements of the fluorescence peak maximum of CPMV lyophilized with trehalose and reconstituted also indicate that the virus remained intact. Microarray binding assays indicated that CPMV particles chemically modified for use as a fluorescent tracer were intact and retained binding specificity after lyophilization in the presence of trehalose. Thus, we demonstrate that functionalized CPMV nanostructures can be stored for the long term, enabling their use in practical sensing applications.

Raviraja N Seetharam et al 2008 Nanotechnology 19 105504 (7pp) doi: 10.1088/0957-4484/19/10/105504
Raviraja N Seetharam1, Amy Szuchmacher Blum2, Carissa M Soto2, Jessica L Whitley3, Kim E Sapsford4, Anju Chatterji5, Tianwei Lin5, John E Johnson5, Charles Guerra1, Peter Satir1 and Banahalli R Ratna2
1 Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA
2 Center for Bio/Molecular Science and Engineering, Naval Research Laboratory, 4555 Overlook Avenue SW, Washington, DC 20375, USA
3 Geo-Centers, Incorporated, Newton, MA 02459, USA
4 George Mason University, 10910 University Boulevard, Manassas, VA 20110, USA
5 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

E-mail: amy.blum@nrl.navy.mil

Print publication: Issue 10 (12 March 2008)
Received 15 August 2007, in final form 10 January 2008
Published 13 February 2008
http://www.iop.org/EJ/abstract/0957-4484/19/10/105504