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778 results on '"Jarrold, Martin F."'

3. Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry

Author

Zhao, Zhongchao, Wang, Joseph Che-Yen, Zhang, Mi, Lyktey, Nicholas A, Jarrold, Martin F, Jacobson, Stephen C, and Zlotnick, Adam

Subjects
Biological Sciences, Chemical Sciences, Physical Chemistry, Infectious Diseases, Bioengineering, Infection, Good Health and Well Being, Capsid, Capsid Proteins, Cryoelectron Microscopy, Hepatitis B virus, Models, Molecular, Protein Multimerization, Recombinant Proteins, Virus Assembly
Abstract

Symmetrical protein complexes are ubiquitous in biology. Many have been re-engineered for chemical and medical applications. Viral capsids and their assembly are frequent platforms for these investigations. A means to create asymmetric capsids may expand applications. Here, starting with homodimeric Hepatitis B Virus capsid protein, we develop a heterodimer, design a hierarchical assembly pathway, and produce asymmetric capsids. In the heterodimer, the two halves have different growth potentials and assemble into hexamers. These preformed hexamers can nucleate co-assembly with other dimers, leading to Janus-like capsids with a small discrete hexamer patch. We can remove the patch specifically and observe asymmetric holey capsids by cryo-EM reconstruction. The resulting hole in the surface can be refilled with fluorescently labeled dimers to regenerate an intact capsid. In this study, we show how an asymmetric subunit can be used to generate an asymmetric particle, creating the potential for a capsid with different surface chemistries.

Published
2021

5. Integrative structure and functional anatomy of a nuclear pore complex

Author

Kim, Seung Joong, Fernandez-Martinez, Javier, Nudelman, Ilona, Shi, Yi, Zhang, Wenzhu, Raveh, Barak, Herricks, Thurston, Slaughter, Brian D, Hogan, Joanna A, Upla, Paula, Chemmama, Ilan E, Pellarin, Riccardo, Echeverria, Ignacia, Shivaraju, Manjunatha, Chaudhury, Azraa S, Wang, Junjie, Williams, Rosemary, Unruh, Jay R, Greenberg, Charles H, Jacobs, Erica Y, Yu, Zhiheng, de la Cruz, M Jason, Mironska, Roxana, Stokes, David L, Aitchison, John D, Jarrold, Martin F, Gerton, Jennifer L, Ludtke, Steven J, Akey, Christopher W, Chait, Brian T, Sali, Andrej, and Rout, Michael P

Subjects
Biochemistry and Cell Biology, Biological Sciences, 1.1 Normal biological development and functioning, Generic health relevance, Cross-Linking Reagents, Mass Spectrometry, Models, Molecular, Nuclear Pore, Nuclear Pore Complex Proteins, Protein Stability, Protein Transport, RNA Transport, Saccharomyces cerevisiae, General Science & Technology
Abstract

Nuclear pore complexes play central roles as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm. However, their large size and dynamic nature have impeded a full structural and functional elucidation. Here we determined the structure of the entire 552-protein nuclear pore complex of the yeast Saccharomyces cerevisiae at sub-nanometre precision by satisfying a wide range of data relating to the molecular arrangement of its constituents. The nuclear pore complex incorporates sturdy diagonal columns and connector cables attached to these columns, imbuing the structure with strength and flexibility. These cables also tie together all other elements of the nuclear pore complex, including membrane-interacting regions, outer rings and RNA-processing platforms. Inwardly directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized into distinct functional units. This integrative structure enables us to rationalize the architecture, transport mechanism and evolutionary origins of the nuclear pore complex.

Published
2018

6. Bortezomib Inhibits Open Configurations of the 20S Proteasome

Author

Henderson, Lucas W., primary, Gautam, Amit K. S., additional, Sharon, Edie M., additional, Johnson, Colin R., additional, Rommel, Nicholas G., additional, Anthony, Adam J., additional, Russell, David H., additional, Jarrold, Martin F., additional, Matouschek, Andreas, additional, and Clemmer, David E., additional

Published
2024
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11. Structural basis for nuclear import of hepatitis B virus (HBV) nucleocapsid core

Author

Yang, Ruoyu, primary, Ko, Ying-Hui, additional, Li, Fenglin, additional, Lokareddy, Ravi K., additional, Hou, Chun-Feng David, additional, Kim, Christine, additional, Klein, Shelby, additional, Antolínez, Santiago, additional, Marín, Juan F., additional, Pérez-Segura, Carolina, additional, Jarrold, Martin F., additional, Zlotnick, Adam, additional, Hadden-Perilla, Jodi A., additional, and Cingolani, Gino, additional

Published
2024
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12. Charge Detection Mass Spectrometry Reveals Favored Structures in the Assembly of Virus-Like Particles: Polymorphism in Norovirus GI.1

Author

Miller, Lohra M., Draper, Benjamin E., Wang, Joseph C.-Y., and Jarrold, Martin F.

Abstract

The main capsid protein (CP) of norovirus, the leading cause of gastroenteritis, is expected to self-assemble into virus-like particles with the same structure as the wild-type virus, a capsid with 180 CPs in a T= 3 icosahedron. Using charge detection mass spectrometry (CD-MS), we find that the norovirus GI.1 variant is structurally promiscuous, forming a wide variety of well-defined structures, some that are icosahedral capsids and others that are not. The structures that are present evolve with time and vary with solution conditions. The presence of icosahedral T= 3 and T= 4 capsids (240 CPs) under some conditions was confirmed by cryo-electron microscopy (cryo-EM). The cryo-EM studies also confirmed the presence of an unexpected prolate geometry based on an elongated T= 4 capsid with 300 CPs. In addition, CD-MS measurements indicate the presence of well-defined peaks with masses corresponding to 420, 480, 600, and 700 CPs. The peak corresponding to 420 CPs is probably due to an icosahedral T= 7 capsid, but this could not be confirmed by cryo-EM. It is possible that the T= 7 particles are too fragile to survive vitrification. There are no mass peaks associated with the T= 9 and T= 12 icosahedra with 540 and 720 CPs. The larger structures with 480, 600, and 700 CPs are not icosahedral; however, their measured charges suggest that they are hollow shells. The use of CD-MS to monitor virus-like particles assembly may have important applications in vaccine development and quality control.

Published
2024
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14. Evidence for High Tc Superconducting Transitions in Isolated Al45- and Al47- Nanoclusters

Author

Cao, Baopeng, Neal, Colleen M., Starace, Anne K., Ovchinnikov, Yurii N., Kresin, Vladimir Z., and Jarrold, Martin F.

Subjects
Condensed Matter - Superconductivity, Physics - Atomic and Molecular Clusters
Abstract

Heat capacities measured for Al45- and Al47- nanoclusters have reproducible jumps at ~ 200 K. These jumps are consistent with theoretical predictions that some clusters with highly degenerate electronic states near the Fermi level will undergo a transition into a high Tc superconducting state. An analysis based on a theoretical treatment of pairing in Al45- and Al47- agrees well with the experimental data in both the value of the critical temperature and in the size and width of the jumps in the heat capacity.

Published
2008

40. Analysis of Keratinocytic Exosomes from Diabetic and Nondiabetic Mice by Charge Detection Mass Spectrometry

Author

Brown, Brooke A., primary, Guda, Poornachander R., additional, Zeng, Xuyao, additional, Anthony, Adam, additional, Couse, Andrew, additional, Barnes, Lauren F., additional, Sharon, Edie M., additional, Trinidad, Jonathan C., additional, Sen, Chandan K., additional, Jarrold, Martin F., additional, Ghatak, Subhadip, additional, and Clemmer, David E., additional

Published
2022
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41. Hysteresis in HBV requires assembly of near-perfect capsids

Author

Starr, Caleb A., Barnes, Lauren F., Jarrold, Martin F., and Zlotnick, Adam

Subjects
Hepatitis B virus, Capsid, Protein Conformation, Virus Assembly, Capsid Proteins, Article
Abstract

Hepatitis B Virus (HBV) must release its contents to initiate infection, making capsid disassembly critical to the viral life cycle. Capsid assembly proceeds through a cascade of weak interactions to yield uniform particles. However, there is a hysteresis to capsid dissociation that allows capsids to persist under conditions where they could not assemble. In this study we have sought to define the basis of hysteresis by examining urea induced dissociation of in vitro assembled HBV capsids. In general, capsid samples show a mixture of two pools, differentiated by stability. Labile capsid dissociation corresponds to a ~5 μM pseudo-critical concentration of assembly (pcc), the same as observed in assembly reactions. Dissociation of the stable pool corresponds to a sub-femtomolar pcc, indicative of hysteresis. The fraction of stable capsids in an assembly reaction increases with the integrity of the Cp preparation and when association is performed in higher ionic strength, which modifies Cp conformation. Labile complexes are more prevalent when assembly conditions yield many kinetically trapped (incomplete and overgrown) products. Cp isolated from stable capsids reassembles into a mixture of stable and labile capsids. These results suggest that hysteresis arises from an ideal capsid lattice, even when some of the substituents in that lattice have defects. Consistent with structural studies that show a subtle difference between Cp dimers and Cp in capsid, we propose that hysteresis arises when HBV capsids undergo a lattice-dependent structural transition.

Published
2022

47. Comparison of analytical techniques to quantitate the capsid content of adeno-associated viral vectors

Author

Werle, Amanda K., primary, Powers, Thomas W., additional, Zobel, James F., additional, Wappelhorst, Caitlin N., additional, Jarrold, Martin F., additional, Lyktey, Nicholas A., additional, Sloan, Courtney D.K., additional, Wolf, Andrew J., additional, Adams-Hall, Sharee, additional, Baldus, Phoebe, additional, and Runnels, Herbert A., additional

Published
2021
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49. Characterization of Recombinant Chimpanzee Adenovirus C68 Low and High-Density Particles: Impact on Determination of Viral Particle Titer

Author

Mullins, Elise K., primary, Powers, Thomas W., additional, Zobel, Jim, additional, Clawson, Kory M., additional, Barnes, Lauren F., additional, Draper, Benjamin E., additional, Zou, Qin, additional, Binder, Joseph J., additional, Dai, Stanley, additional, Zhang, Kun, additional, Friese, Olga, additional, Runnels, Herbert A., additional, Jarrold, Martin F., additional, and Thompson, Lawrence C., additional

Published
2021
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