The structures of polyoma virus and its polymorphic aggregates, SV40 virus, myosin subfragment-1, and the chloroplast cytochrome b6/f complex will be studied by electron microscopy and image analysis methods. These studies are aimed at answering questions about the overall structure, assembly, stability, and function of these macromolecular aggregates. We will learn about protein-protein interactions in polyoma, SV40, myosin subfragment-1, and cytochrome b6/f, protein-nucleic acid associations in polyoma and SV40, and protein-lipid associations in cytochrome b6/f. The biological significance of each of these systems is well documented. Polyoma and SV40 do not cause malignancies in their natural hosts (mice and rhesus monkeys), but their oncogenic potential is revealed when high concentrations of virus are injected into either foreign hosts or natural hosts lacking a functional immunological system. Subfragment-1, the head portion of myosin, is responsible for force generation in muscle through the hydrolysis of ATP and interaction with actin. Cytochrome b6/f, an integral membrane-spanning complex in chloroplast thylakoids, is involved in photosynthetic and respiratory energy transduction. The potential to study these and similar structures requires continued efforts to develop and implement new techniques of electron microscopy and image analysis as well as the application of established procedures. Microscopy of frozen-hydrated specimens will help reveal the """"""""native"""""""" structure of biological molecules, and implementation of highly interactive, computer graphics image analysis routines will allow flexible and efficient processing of micrographs from a greater variety of biological systems of increased complexity.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM033050-06
Application #
3282398
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1983-06-01
Project End
1991-05-31
Budget Start
1988-06-01
Budget End
1989-05-31
Support Year
6
Fiscal Year
1988
Total Cost
Indirect Cost
Name
Purdue University
Department
Type
Schools of Arts and Sciences
DUNS #
072051394
City
West Lafayette
State
IN
Country
United States
Zip Code
47907
Tan, Yong Zi; Aiyer, Sriram; Mietzsch, Mario et al. (2018) Sub-2?Å Ewald curvature corrected structure of an AAV2 capsid variant. Nat Commun 9:3628
Subramanian, Rohit H; Smith, Sarah J; Alberstein, Robert G et al. (2018) Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions. ACS Cent Sci 4:1578-1586
Nibert, Max L (2017) Mitovirus UGA(Trp) codon usage parallels that of host mitochondria. Virology 507:96-100
Pittman, Nikéa; Misseldine, Adam; Geilen, Lorena et al. (2017) Atomic Resolution Structure of the Oncolytic Parvovirus LuIII by Electron Microscopy and 3D Image Reconstruction. Viruses 9:
Pyle, Jesse D; Keeling, Patrick J; Nibert, Max L (2017) Amalga-like virus infecting Antonospora locustae, a microsporidian pathogen of grasshoppers, plus related viruses associated with other arthropods. Virus Res 233:95-104
Mietzsch, Mario; Kailasan, Shweta; Garrison, Jamie et al. (2017) Structural Insights into Human Bocaparvoviruses. J Virol 91:
Vong, Minh; Ludington, Jacob G; Ward, Honorine D et al. (2017) Complete cryspovirus genome sequences from Cryptosporidium parvum isolate Iowa. Arch Virol 162:2875-2879
Depierreux, Delphine; Vong, Minh; Nibert, Max L (2016) Nucleotide sequence of Zygosaccharomyces bailii virus Z: Evidence for +1 programmed ribosomal frameshifting and for assignment to family Amalgaviridae. Virus Res 217:115-24
Nibert, Max L; Pyle, Jesse D; Firth, Andrew E (2016) A +1 ribosomal frameshifting motif prevalent among plant amalgaviruses. Virology 498:201-208
Li, Zhihai; Yan, Xiaodong; Yu, Hai et al. (2016) The C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host Interaction. Structure 24:874-85

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