This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A virtually universal property of viruses is the requirement for the virus coat to make the transition from being an inert rigid protective outer coating to an activated dynamic particle capable of nucleic acid delivery during infection. This dynamic process requires conformational changes in the virus coat (Poranen, Daugelavicius, and Bamford, 2002) (Dryden et al., 1993;Endrich, Gehrig, and Gehrig, 1999;Fuller and Lee, 1992;Kirnbauer et al., 1993). However few mechanistic details are available about this essential process because of a lack of a model research system, an easily detectable phenotype and an assay for their detection. The bacterial virus MS2 is exceptional for its simplicity. MS2 is a 24nm icosahedral virus composed of only two proteins, 180 copies of coat protein(Mr=13.7KDa), a single copy of a maturation protein called A (Mr=44KDa) as well as a single stranded genomic RNA. As a result, it is a well characterized genetic and biochemical system (Golmoham madi et al., 1993;Konig et al., 2003;Ni et al., 1995;Stonehouse and Stockley, 1993;Stonehouse et al., 1996;Valegard et al., 1990;Valegard et al., 1991;Valegard et al., 1997;Valegard et al., 1986;van den Worm et al., 2006). Recently, our group has shown that the coat undergoes coat-specific changes in thickness during infection which we hypothesize are mediated by a single protein, A, using small angle scattering techniques in solution(Kuzmanovic et al., 2006b). Although, the change in thickness as measured by small angle neutron scattering (SANS) is dramatic, 21A to 31A in the absence A protein, these changes have not been observed previously using either cryo-EM or X-ray crystallography (Kuzmanovic et al., 2006b) (Golmohammadi et al., 1993;(Toropova et al., 2008)

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR017573-08
Application #
7956460
Study Section
Special Emphasis Panel (ZRG1-CB-B (40))
Project Start
2009-05-01
Project End
2010-04-30
Budget Start
2009-05-01
Budget End
2010-04-30
Support Year
8
Fiscal Year
2009
Total Cost
$12,892
Indirect Cost
Name
Scripps Research Institute
Department
Type
DUNS #
781613492
City
La Jolla
State
CA
Country
United States
Zip Code
92037
Scapin, Giovanna; Dandey, Venkata P; Zhang, Zhening et al. (2018) Structure of the insulin receptor-insulin complex by single-particle cryo-EM analysis. Nature 556:122-125
Sherman, Michael B; Kakani, Kishore; Rochon, D'Ann et al. (2017) Stability of Cucumber Necrosis Virus at the Quasi-6-Fold Axis Affects Zoospore Transmission. J Virol 91:
Geary, Cody; Chworos, Arkadiusz; Verzemnieks, Erik et al. (2017) Composing RNA Nanostructures from a Syntax of RNA Structural Modules. Nano Lett 17:7095-7101
Kulczyk, Arkadiusz W; Moeller, Arne; Meyer, Peter et al. (2017) Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis. Proc Natl Acad Sci U S A 114:E1848-E1856
Razinkov, Ivan; Dandey, Venkat; Wei, Hui et al. (2016) A new method for vitrifying samples for cryoEM. J Struct Biol 195:190-198
Short, James R; Speir, Jeffrey A; Gopal, Radhika et al. (2016) Role of Mitochondrial Membrane Spherules in Flock House Virus Replication. J Virol 90:3676-83
Lee, Jeong Hyun; Leaman, Daniel P; Kim, Arthur S et al. (2015) Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike. Nat Commun 6:8167
Derking, Ronald; Ozorowski, Gabriel; Sliepen, Kwinten et al. (2015) Comprehensive antigenic map of a cleaved soluble HIV-1 envelope trimer. PLoS Pathog 11:e1004767
Guenaga, Javier; de Val, Natalia; Tran, Karen et al. (2015) Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like properties. PLoS Pathog 11:e1004570
McCullough, John; Clippinger, Amy K; Talledge, Nathaniel et al. (2015) Structure and membrane remodeling activity of ESCRT-III helical polymers. Science 350:1548-51

Showing the most recent 10 out of 189 publications