Jared Pitts 1 protocol

Janna Bigalke Department of Molecular Biology and Microbiology, Tufts University School of Medicine, USA
1 protocol

Ekaterina Heldwein
  • Associate Professor with tenure, Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA
Research focus
  • Microbiology
  • 2 Author merit

Education

PhD, Biochemistry, Oregon Health and Sciences University, 1999

Publications

Since 2006
• Draganova E. B., Zhang J., Zhou Z. H., and Heldwein E. E. (2020). Structural basis for capsid recruitment and coat formation during HSV-1 nuclear egress. BIORXIV/2020/988170.
• Hilterbrand, A.T., Daly R., and Heldwein E.E. (2020). Contributions of the four essential entry glycoproteins to HSV-1 tropism and the selection of entry routes. BIORXIV/2020/985325.
• Cooper, R.S. and Heldwein E. E. (2020). Expression, purification, and crystallization of full-length HSV-1 gB for structure determination. In “Methods in Molecular Biology: Herpes Simplex Virus: Methods and Protocols”, R. Diefenbach and C. Fraefel, Eds. Springer Science and Business Media. 2060:395-407.
• White, E. M., Stampfer, S. D., and Heldwein E. E. (2020). Expression, purification, and crystallization of HSV-1 glycoproteins for structure determination. In “Methods in Molecular Biology: Herpes Simplex Virus: Methods and Protocols”, R. Diefenbach and C. Fraefel, Eds. Springer Science and Business Media. 2060:377-393.
• Hilterbrand A. T. and Heldwein E. E. (2019). Go go gadget glycoprotein!: HSV-1 draws on its sizeable glycoprotein tool kit to customize its diverse entry routes. PLOS Pathogens 15: e1007660.
• Koenigsberg, A. L. and Heldwein E. E. (2018). The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem. 293, 15827-15839.
• Cooper, R.C., Georgieva, E. R., Borbat, P. P., Freed, J. H., and Heldwein E. E. (2018). Structural basis for membrane anchoring and fusion regulation of the Herpes Simplex Virus fusogen gB. Nat Struct Mol Biol 25, 416-424.
• Richards, A. L., Sollars, P. J., Pitts, J. D., Stults, A. M., Heldwein, E. E., Pickard, G. E., and Smith G.A. (2017). The pUL37 tegument protein guides microtubule transport to promote alpha-herpesvirus neuroinvasion. PLOS Pathogens 13: e1006741.
• Koenigsberg, A. L. and Heldwein, E. E. (2017). Crystal structure of the N-terminal half of the traffic controller UL37 from Herpes Simplex virus Type 1. J Virol 91: e01244-17.
• Wang, P., Yu, Z., Santangelo, T. J., Olesik, J., Wang, Y., Heldwein, E. E. and Li, X. (2017). BosR Is a Novel Fur Family Member Responsive to Copper and Regulating Copper Homeostasis in Borrelia burgdorferi. J Bact 199: e00276-17.
• Bigalke, J. M. and Heldwein, E. E. (2017). Have NEC coat, will travel: structural basis of membrane budding during nuclear egress in herpesviruses. In “Advances in Virus Research”, M. Kielian, T.C. Mettenleiter, and M.J. Roossinck, Eds. Academic Press. 2017: 97:107-141.
• Rogalin, H. B. and Heldwein, E. E. (2016). Characterization of VSV pseudotypes bearing essential entry glycoproteins gB, gD, gH, and gL of Herpes Simplex virus Type 1. J Virol 90:10321-10328.
• Bigalke, J. M. and Heldwein E. E. (2016). Expression, Purification and Crystallization of the Herpesvirus Nuclear Egress Complex (NEC). Bio-protocol. 6: e1872.
• Metrick, C. M. and Heldwein E. E. (2016). The novel structure and unexpected RNA-binding ability of the C-terminal domain of HSV-1 tegument protein UL21. J Virol 90:5759-5769.
• Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D. et al. (2016). Data publication with the structural biology data grid supports live analysis. Nat Commun 7: 10882.
• Bigalke, J. M. and Heldwein, E. E. (2015). Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J 34(23): 2921-2936.
• Burke, H. G. and Heldwein, E. E. (2015). Crystal Structure of the Human Cytomegalovirus Glycoprotein B. PLoS Pathog 11(10): e1005227.
• Rogalin, H. B. and Heldwein, E. E. (2015). Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion. J Virol 89(24): 12262-12272.
• Metrick, C. M., Chadha, P. and Heldwein, E. E. (2015). The unusual fold of herpes simplex virus 1 UL21, a multifunctional tegument protein. J Virol 89(5): 2979-2984.
• Bigalke, J. M., Heuser, T., Nicastro, D. and Heldwein, E. E. (2014). Membrane deformation and scission by the HSV-1 nuclear egress complex. Nat Commun 5: 4131.
• Pitts, J. D., Klabis, J., Richards, A. L., Smith, G. A. and Heldwein, E. E. (2014). Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking. J Virol 88(10): 5462-5473.
• Silverman, J. L. and Heldwein, E. E. (2013). Mutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells. J Virol 87(18): 10139-10147.
• Vitu, E., Sharma, S., Stampfer, S. D. and Heldwein, E. E. (2013). Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form. J Mol Biol425(11): 2056-2071.
• Sharma, S., Wisner, T. W., Johnson, D. C. and Heldwein, E. E. (2013). HCMV gB shares structural and functional properties with gB proteins from other herpesviruses.Virology 435(2): 239-249.
• Silverman, J. L., Greene, N. G., King, D. S. and Heldwein, E. E. (2012). Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation. J Virol 86(15): 8171-8184.
• Cairns, T. M., Whitbeck, J. C., Lou, H., Heldwein, E. E., Chowdary, T. K., Eisenberg, R. J. and Cohen, G. H. (2011). Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment. J Virol 85(13): 6175-6184.
• Stampfer, S. D., Lou, H., Cohen, G. H., Eisenberg, R. J. and Heldwein, E. E. (2010). Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. J Virol 84(24): 12924-12933.
• Chowdary, T. K., Cairns, T. M., Atanasiu, D., Cohen, G. H., Eisenberg, R. J. and Heldwein, E. E. (2010). Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL. Nat Struct Mol Biol 17(7): 882-888.
• Chowdary, T. K. and Heldwein, E. E. (2010). Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions. J Virol 84(10): 4923-4935.
• Silverman, J. L., Sharma, S., Cairns, T. M. and Heldwein, E. E. (2010). Fusion-deficient insertion mutants of herpes simplex virus type 1 glycoprotein B adopt the trimeric postfusion conformation. J Virol 84(4): 2001-2012.
• Hannah, B. P., Heldwein, E. E., Bender, F. C., Cohen, G. H. and Eisenberg, R. J. (2007). Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B. J Virol 81(9): 4858-4865.
• Bender, F. C., Samanta, M., Heldwein, E. E., de Leon, M. P., Bilman, E., Lou, H., Whitbeck, J. C., Eisenberg, R. J. and Cohen, G. H. (2007). Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions. J Virol 81(8): 3827-3841.
• Heldwein, E. E., Lou, H., Bender, F. C., Cohen, G. H., Eisenberg, R. J. and Harrison, S. C. (2006). Crystal structure of glycoprotein B from herpes simplex virus 1. Science313(5784): 217-220.
2 Protocols published
Identification of Buffer Conditions for Optimal Thermostability and Solubility of Herpesviral Protein UL37 Using the Thermofluor Assay
Authors:  Andrea L. Koenigsberg, Jared D. Pitts and Ekaterina E. Heldwein, date: 06/20/2020, view: 717, Q&A: 0
Structural and biochemical studies of proteins require high amounts of stable, purified proteins. Protein stability often depends on the buffer composition, which includes pH and concentration of salts or other solutes such as glycerol, hence an ...
Expression, Purification and Crystallization of the Herpesvirus Nuclear Egress Complex (NEC)
Authors:  Janna M. Bigalke and Ekaterina E. Heldwein, date: 07/20/2016, view: 5957, Q&A: 0
The protocol describes the production and crystallization of the soluble form of the nuclear egress complex (NEC) from Herpes simplex virus 1 and Pseudorabies virus. The NEC is a heterodimer that consists of conserved proteins UL31 and UL34. NEC ...
We use cookies on this site to enhance your user experience. By using our website, you are agreeing to allow the storage of cookies on your computer.