This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Bacteriophage Epsilon15 is a generalized transducing phage infecting the human/animal pathogen Salmonella enterica serovar Anatum. Epsilon 15 has been studied for its ability to recognize and bind O-antigen as well as its capacity to alter host lipopolysaccharide in the lysogenic state. The viral protein responsible for O-antigen recognition is the tailspike protein. The virion contains at least six structural proteins and an approximately 40 kb dsDNA genome of known sequence. At the sequence level, the structural proteins most closely resemble the Bcep phages of Burkholderia, a human pathogen affecting cystic fibrosis patients. The virion structural proteins and chromosome together make a particle with a mass of approximately 66 Megadaltons and a diameter of roughly 6500 ?. Jon King's lab has used mass spectrometric methods to identify those open reading frames encoding virion structural proteins. The structure of this virus will reveal the arrangement of structural proteins and, in particular, the configuration of those subunits more directly involved in attachment to the host and passage of DNA into the cytoplasm. A genetic approach is now underway to isolate amber mutants in virus structural proteins. Macromolecular subassemblies formed during infections with these mutant phage will be purified and imaged by reconstruction. These mutant phage will also serve as reagents for imaging the interactions between virus and lipopolysaccharide and receptor proteins at the surface of the host.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biotechnology Resource Grants (P41)
Project #
Application #
Study Section
Special Emphasis Panel (ZRG1-BCMB-T (41))
Project Start
Project End
Budget Start
Budget End
Support Year
Fiscal Year
Total Cost
Indirect Cost
Baylor College of Medicine
Schools of Medicine
United States
Zip Code
Wensel, Theodore G; Zhang, Zhixian; Anastassov, Ivan A et al. (2016) Structural and molecular bases of rod photoreceptor morphogenesis and disease. Prog Retin Eye Res 55:32-51
Ebeida, Mohamed S; Rushdi, Ahmad A; Awad, Muhammad A et al. (2016) Disk Density Tuning of a Maximal Random Packing. Comput Graph Forum 35:259-269
Bucero, Marta Abril; Bajaj, Chandrajit; Mourrain, Bernard (2016) On the construction of general cubature formula by flat extensions. Linear Algebra Appl 502:104-125
Zhang, Qin; Cha, Deukhyun; Bajaj, Chandrajit (2015) Quality Partitioned Meshing of Multi-Material Objects. Procedia Eng 124:187-199
Baranovskiy, Andrey G; Zhang, Yinbo; Suwa, Yoshiaki et al. (2015) Crystal structure of the human primase. J Biol Chem 290:5635-46
Wensel, Theodore G; Gilliam, Jared C (2015) Three-dimensional architecture of murine rod cilium revealed by cryo-EM. Methods Mol Biol 1271:267-92
Bettadapura, Radhakrishna; Rasheed, Muhibur; Vollrath, Antje et al. (2015) PF2fit: Polar Fast Fourier Matched Alignment of Atomistic Structures with 3D Electron Microscopy Maps. PLoS Comput Biol 11:e1004289
Baker, Mariah R; Fan, Guizhen; Serysheva, Irina I (2015) Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous Environment. Eur J Transl Myol 25:4803
Edwards, John; Daniel, Eric; Pascucci, Valerio et al. (2015) Approximating the Generalized Voronoi Diagram of Closely Spaced Objects. Comput Graph Forum 34:299-309
Baker, Mariah R; Fan, Guizhen; Serysheva, Irina I (2015) Single-particle cryo-EM of the ryanodine receptor channel in an aqueous environment. Eur J Transl Myol 25:35-48

Showing the most recent 10 out of 210 publications