David M. Belnap

David M. Belnap, PhD, BS

Languages spoken: English

Academic Information

Departments Primary - Biochemistry

Academic Office Information

david.belnap@utah.edu

I currently serve as the director of the Electron Microscopy Core Laboratory at the University of Utah, where I help many people image their samples, advise people on electron microscopy experiments, and maintain and manage the laboratory. As personal research interests, I am interested in the structure, function, assembly, and disassembly of viruses and cellular macromolecules. I am particularly interested in using structural techniques to understand virus cell-entry, assembly, and evolution. My primary research tool is cryogenic electron microscopy and three-dimensional reconstruction (cryo-EM), in addition to the (often) preparatory technique of negative-staining electron microscopy. I am also interested in improving cryo-EM techniques.

Research Statement

I am interested in the structure, function, assembly, and disassembly of viruses and cellular macromolecules. I am particularly interested in using structural techniques to understand virus cell-entry, assembly, and evolution. My primary research tool is cryogenic electron microscopy and three-dimensional reconstruction (cryo-EM). I am also interested in improving cryo-EM techniques. I currently serve as the director of the Electron Microscopy Core Laboratory at the University of Utah, where I work with many to help them image their samples. I am happy to be of service to them.

Education History

Undergraduate Brigham Young University
 BS
Doctoral Training Purdue University
 PhD
Postdoctoral Fellowship National Institutes of Health
 Postdoctoral Fellow

Selected Publications

Journal Article

  1. Skliar M, Chernyshev VS, Belnap DM, Sergey GV, Al-Hakami SM, Bernard PS, Stijleman IJ, Rachamadugu R (2018). Membrane proteins significantly restrict exosome mobility. Biochem Biophys Res Commun, 501, 1055-1059.
  2. Budzinski KL, Allen RW, Fujimoto BS, Kensel-Hammes P, Belnap DM, Bajjalieh SM, Chiu DT (2009). Large structural change in isolated synaptic vesicles upon loading with neurotransmitter. Biophys J, 97(9), 2577-84. (Read full article)
  3. Belnap DM, Olson NH, Baker TS (1997). A method for establishing the handedness of biological macromolecules. J Struct Biol, 120(1), 44-51. (Read full article)
  4. Beuron F, Maurizi MR, Belnap DM, Kocsis E, Booy FP, Kessel M, Steven AC (1998). At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J Struct Biol, 123(3), 248-59. (Read full article)
  5. Belnap DM, Kumar A, Folk JT, Smith TJ, Baker TS (1999). Low-resolution density maps from atomic models: how stepping "back" can be a step "forward". J Struct Biol, 125(2-3), 166-75. (Read full article)
  6. Caston JR, Belnap DM, Steven AC, Trus BL (1999). A strategy for determining the orientations of refractory particles for reconstruction from cryo-electron micrographs with particular reference to round, smooth-surfaced, icosahedral viruses. J Struct Biol, 125(2-3), 209-15. (Read full article)
  7. Heymann JB, Belnap DM (2007). Bsoft: image processing and molecular modeling for electron microscopy. J Struct Biol, 157(1), 3-18. (Read full article)
  8. Sanz-Garcia E, Stewart AB, Belnap DM (2010). The random-model method enables ab initio 3D reconstruction of asymmetric particles and determination of particle symmetry. J Struct Biol, 171(2), 216-22. (Read full article)
  9. Heymann JB, Chagoyen M, Belnap DM (2005). Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology. J Struct Biol, 151(2), 196-207.
  10. Heymann JB, Chagoyen M, Belnap DM (2006). Corrigendum to ¿Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology¿ [J. Struct. Biol. 151 (2005) 196¿207]. J Struct Biol, 153(3), 312.
  11. Pastuzyn ED, Day CE, Kearns RB, Kyrke-Smith M, Taibi AV, McCormick J, Yoder N, Belnap DM, Erlendsson S, Morado DR, Briggs JAG, Feschotte C, and Shepherd JD (2018). The neuronal gene Arc encodes a repurposed retrotransposon Gag protein that mediates trans-cellular RNA transfer. Cell, 172, 275-288.
  12. Watts NR, Conway JF, Cheng N, Stahl SJ, Belnap DM, Steven AC, Wingfield PT (2002). The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface. EMBO J, 21(5), 876-84. (Read full article)
  13. Heymann JB, Iwasaki K, Yim YI, Cheng N, Belnap DM, Greene LE, Eisenberg E, Steven AC (2005). Visualization of the binding of Hsc70 ATPase to clathrin baskets: implications for an uncoating mechanism. J Biol Chem, 280(8), 7156-61. (Read full article)
  14. Lin J, Cheng N, Hogle JM, Steven AC, Belnap DM (2013). Conformational Shift of a Major Poliovirus Antigen Confirmed by Immuno-Cryogenic Electron Microscopy. J Immunol, 191(2), 884-991.
  15. Belnap DM, Olson NH, Cladel NM, Newcomb WW, Brown JC, Kreider JW, Christensen ND, Baker TS (1996). Conserved features in papillomavirus and polyomavirus capsids. J Mol Biol, 259(2), 249-63. (Read full article)
  16. Conway JF, Cheng N, Zlotnick A, Stahl SJ, Wingfield PT, Belnap DM, Kanngiesser U, Noah M, Steven AC (1998). Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens. J Mol Biol, 279(5), 1111-21. (Read full article)
  17. Harris A, Belnap DM, Watts NR, Conway JF, Cheng N, Stahl SJ, Vethanayagam JG, Wingfield PT, Steven AC (2006). Epitope diversity of hepatitis B virus capsids: quasi-equivalent variations in spike epitopes and binding of different antibodies to the same epitope. J Mol Biol, 355(3), 562-76. (Read full article)
  18. Belnap DM, Filman DJ, Trus BL, Cheng N, Booy FP, Conway JF, Curry S, Hiremath CN, Tsang SK, Steven AC, Hogle JM (2000). Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus. J Virol, 74(3), 1342-54. (Read full article)
  19. Cheng N, Trus BL, Belnap DM, Newcomb WW, Brown JC, Steven AC (2002). Handedness of the herpes simplex virus capsid and procapsid. J Virol, 76(15), 7855-9. (Read full article)
  20. Conway JF, Watts NR, Belnap DM, Cheng N, Stahl SJ, Wingfield PT, Steven AC (2003). Characterization of a conformational epitope on hepatitis B virus core antigen and quasiequivalent variations in antibody binding. J Virol, 77(11), 6466-73. (Read full article)
  21. Bubeck D, Filman DJ, Cheng N, Steven AC, Hogle JM, Belnap DM (2005). The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J Virol, 79(12), 7745-55. (Read full article)
  22. Lin J, Cheng N, Chow M, Filman DJ, Steven AC, Hogle JM, Belnap DM (2011). An externalized polypeptide partitions between two distinct sites on genome-released poliovirus particles. J Virol, 85(19), 9974-83. (Read full article)
  23. Shen PS, Domek MJ, Sanz-Garcia E, Makaju A, Taylor RM, Hoggan R, Culumber MD, Oberg CJ, Breakwell DP, Prince JT, Belnap DM (2012). Sequence and Structural Characterization of Great Salt Lake Bacteriophage CW02, a Member of the T7-Like Supergroup. J Virol, 86(15), 7907-17. (Read full article)
  24. Grose JH, Belnap DM, Jensen JD, Mathis AD, Prince JT, Burnett SH, and Breakwell DP (2014). The genomes, proteomes and structure of three novel phages that infect the Bacillus cereus group and carry putative virulence factors. J Virol, 88, 11846-11860.
  25. Lin J, Lee LY, Roivainen M, Filman DJ, Hogle JM, Belnap DM (2012). Structure of the Fab-labeled "breathing" state of native poliovirus. J Virol, 86(10), 5959-62. J Virol, 86(10), 5959-5962.
  26. Strauss M, Filman DJ, Belnap DM, Cheng N, Noel RT, and Hogle JM (2015). Nectin-like interactions between poliovirus and its receptor trigger conformational changes associated with cell entry. J Virol, 89, 4143-4157.
  27. Ishikawa T, Maurizi MR, Belnap D, Steven AC (2000). Docking of components in a bacterial complex. Nature, 408(6813), 667-8. (Read full article)
  28. Votteler J, Ogohara C, Yi S, Hsia Y, Nattermann U, Belnap DM, King NP, and Sundquist WI (2016). Designed proteins induce the formation of nanocage-containing extracellular vesicles. Nature, 540, 292-295.
  29. Carragher BO, Cheng N, Wang ZY, Korn ED, Reilein A, Belnap DM, Hammer JA 3rd, Steven AC (1998). Structural invariance of constitutively active and inactive mutants of acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states. Proc Natl Acad Sci U S A, 95(26), 15206-11. (Read full article)
  30. Belnap DM, McDermott BM Jr, Filman DJ, Cheng N, Trus BL, Zuccola HJ, Racaniello VR, Hogle JM, Steven AC (2000). Three-dimensional structure of poliovirus receptor bound to poliovirus. Proc Natl Acad Sci U S A, 97(1), 73-8. (Read full article)
  31. Belnap DM, Watts NR, Conway JF, Cheng N, Stahl SJ, Wingfield PT, Steven AC (2003). Diversity of core antigen epitopes of hepatitis B virus. Proc Natl Acad Sci U S A, 100(19), 10884-9. (Read full article)
  32. Grunewald K, Desai P, Winkler DC, Heymann JB, Belnap DM, Baumeister W, Steven AC (2003). Three-dimensional structure of herpes simplex virus from cryo-electron tomography. Science, 302(5649), 1396-8. (Read full article)
  33. Belnap DM, Grochulski WD, Olson NH, Baker TS (1993). Use of radial density plots to calibrate image magnification for frozen-hydrated specimens. Ultramicroscopy, 48(3), 347-58. (Read full article)
  34. Lattin JR, Pitt WG, Belnap DM, Husseini GA (2012). Ultrasound-induced calcein release from eLiposomes. Ultrasound Med Biol, 38, 2163-2173.
  35. Thomas JA, Rolando MR, Carroll CA, Shen PS, Belnap DM, Weintraub ST, Serwer P, Hardies SC (2008). Characterization of Pseudomonas chlororaphis myovirus 201varphi2-1 via genomic sequencing, mass spectrometry, and electron microscopy. Virology, 376(2), 330-8. (Read full article)
  36. Shen PS, Enderlein D, Nelson CD, Carter WS, Kawano M, Xing L, Swenson RD, Olson NH, Baker TS, Cheng RH, Atwood WJ, Johne R, Belnap DM (2011). The structure of avian polyomavirus reveals variably sized capsids, non-conserved inter-capsomere interactions, and a possible location of the minor capsid protein VP4. Virology, 411(1), 142-52. (Read full article)
  37. Johne R, Otto P, Roth B, Löhrend U, Belnap D, Reetza J, Trojnar E (2011). Sequence analysis of the VP6-encoding genome segment of avian group F and G rotaviruses. Virology, 412, 384-391.
  38. Lattin JR, Belnap DM, Pitt WG (2012). Formation of eLiposomes as a drug delivery vehicle. Colloids Surf B Biointerfaces, 89, 93-100. (Read full article)
  39. Javadi M, Pitt WG, Belnap DM, Tsosie NH, Hartley JM (2012). Encapsulating nanoemulsions inside eLiposomes for ultrasonic drug delivery. Langmuir, 28, 14720-14729.
  40. Chernyshev VS, Rachamadugu R, Tseng YH, Belnap DM, Jia Y, Branch KJ, Butterfield AE, Pease LF III, Bernard PS, and Skliar M (2015). Size and shape characterization of hydrated and desiccated exosomes. Anal Bioanal Chem, 407(12), 3285-3301.
  41. Hamblin MN, Xuan J, Maynes D, Tolley HD, Belnap DM, Woolley AT, Lee ML, Hawkins AR (2010). Selective trapping and concentration of nanoparticles and viruses in dual-height nanofluidic channels. Lab Chip, 10(2), 173-8. (Read full article)
  42. Lin CY, Javadi M, Belnap DM, Barrow J, and Pitt WG (2014). Ultrasound sensitive eLiposomes containing doxorubicin for drug targeting therapy. Nanomedicine, 10, 67-76.
  43. Saha I, Preece B, Peterson A, Durden H, MacArthur B, Lowe J, Belnap D, Vershinin M, Saffarian S (2021). Gag-Gag interactions are insufficient to fully stabilize and order the immature HIV Gag lattice. Viruses, 13, 1946.
  44. Aquino Neto S, Almeida TS, Belnap DM, Minteer SD, De Andrade AR (2015). Enhanced reduced nicotinamide adenine dinucleotide electrocatalysis onto multi-walled carbon nanotubes-decorated gold nanoparticles and their use in hybrid biofuel cell. J Power Sources, 273, 1065-1072.
  45. Heather Swann, Abhimanyu Sharma, Benjamin Preece, Abby Peterson, Crystal Eldridge, David M. Belnap, Michael Vershinin, and Saveez Saffarian (2020). Minimal system for assembly of SARS-CoV-2 virus like particles. Sci Rep, 10, 21877.
  46. Swann H, Sharma A, Preece B, Peterson A, Eldridge C, Belnap DM, Vershinin M, Saffarian (2021). Minimal system for assembly of SARS-CoV-2 virus like particles (author correction). Scientific reports, 11, 9352.
  47. Barnard, D.L., Belnap, D.M., Azadi, P., Heiss, C., Snyder, D.S., Bock, S.C., and Konowalchuk, T.W (2022). Examining the interactions of GalahadTM compound with viruses to develop a novel inactivated influenza A virus vaccine. Heliyon, 8, e09887.
  48. Wardzala CL, Wood AM, Belnap DM, Kramer J (2022). Mucins Inhibit Coronavirus Infection in a Glycan-Dependent Manner. ACS central science, 8(3), 351-360. (Read full article)
  49. Momont C, Dang HV, Zatta F, Hauser K, Wang C, di Iulio J, Minola A, Czudnochowski N, De Marco A, Branch K, Donermeyer D, Vyas S, Chen A, Ferri E, Guarino B, Powell AE, Spreafico R, Yim SS, Balce DR, Bartha I, Meury M, Croll TI, Belnap DM, Schmid MA, Schaiff WT, Miller JL, Cameroni E, Telenti A, Virgin HW, Rosen LE, Purcell LA, Lanzavecchia A, Snell G, Corti D, Pizzuto M (2023). A pan-influenza antibody inhibiting neuraminidase via receptor mimicry. Nature, 618(7965), 590-597. (Read full article)
  50. Lempp FA, Volz T, Cameroni E, Benigni F, Zhou J, Rosen LE, Noack J, Zatta F, Kaiser H, Bianchi S, Lombardo G, Jaconi S, Vincenzetti L, Imam H, Soriaga LB, Passini N, Belnap DM, Schulze A, Lütgehetmann M, Telenti A, Cathcart AL, Snell G, Purcell LA, Hebner CM, Urban S, Dandri M, Corti D, Schmid M (2023). Potent broadly neutralizing antibody VIR-3434 controls hepatitis B and D virus infection and reduces HBsAg in humanized mice. Journal of hepatology, 79(5), 1129-1138. (Read full article)
  51. Backman, T., Latorre. S.M., Symeonidi, E., Muszy'ski, A., Bleak, E., Eads, L., Martinez-Koury. P.I., Som, S., Hawks, A., Gloss, A.D., Belnap, D.M., Manuel, A.M., Deutschbauer, A.M., Bergelson, J,, Azadi, P., Burbano, H.A., Karasov, T.L (2024). A phage tail-like bacteriocin suppresses competitors in metapopulations of pathogenic bacteria. Science, 384(6701), eado0713.
  52. Backman, T., Latorre. S.M., Symeonidi, E., Muszy¿ski, A., Bleak, E., Eads, L., Martinez-Koury. P.I., Som, S., Hawks, A., Gloss, A.D., Belnap, D.M., Manuel, A.M., Deutschbauer, A.M., Bergelson, J,, Azadi, P., Burbano, H.A., Karasov, T.L (2025). Erratum for the Research Article “A phage tail–like bacteriocin suppresses competitors in metapopulations of pathogenic bacteria” by T. Backman et al. Science, 388(6743), eadx9434.
  53. Preece, B., Peppel, W., Gallegos, R., Ysassi, G., Clinger, G., Bohn, N., Adhikary, B., Mendonça, L., Belnap, D., Vershinin, M., Saffarian S (2025). High-yield and quantitative purification method for HIV which minimizes forces applied to virions utilized to investigate maturation of HIV-1 via cryo-electron tomography. Viruses, 17(3), 364.
  54. Vincenzetti, L., Wong, R., Marzi, R., Guarino, B., Stefanutti, E., Gupta, S. V., Rosen, L. E., Belnap, D. M., Wang, L., Chen, Y. P., di Iulio, J., Momin, A., Tracy, K. E., Deshpande, S., Errico, J. M., Giovannoni, F., Sprugasci, N., Peter, A., Seu, L., Cloutier, D., Tay, C.H., Snell, G., Czudnochowski, N., Lempp, F.A., Havenar-Daughton, C., Benigni, F., Lanzavecchia, A., Agarwal, K., Yuen, M.F., Wedemeyer, H., Gane, E., Arvin, A., Corti, D., Schmid, M. A (2025). Engineered monoclonal antibody tobevibart enhances HBsAg capture by Fc receptor-positive cells and activates HBV-specific T cells. Journal of hepatology, 84(1), 62¿73.
  55. Powell, A.E., Caruso, H., Park, S., Chen, J.-L., O'Rear, J., Ferrer, B.J., Stieh, D.J., Weiss, A.M., Belnap, D.M., Walker, A., Bruening, A., Hartwig, A., Sprouse, K.R., Addetia, A., Alshukairi, A.N., Ahyong, V., Dougherty, C.S., Veesler, D., Bowen, R., Ledgerwood, J.E., Kay, M.S., Weidenbacher, P.A.-B., Palanski, B.A A stabilized MERS-CoV spike ferritin nanoparticle vaccine elicits robust and protective neutralizing antibody responses. Nature communications,
  56. Masubuchi, T., Rublev, P., Han, Y., Perez, J.P.L., Boebinger, M., Hwang, S., Saravanan, L., Belnap, D.M., Alexandrova, A.N., Anderson, S.L (2025). Highly active hydrogen evolution reaction (HER) catalysts formed by energetic Ptn cluster deposition: Deposition dynamics and the HER mechanism. Journal of the American Chemical Society, in press.

Review

  1. Belnap DM, Steven AC (2000). 'Deja vu all over again': the similar structures of bacteriophage PRD1 and adenovirus. [Review]. Trends Microbiol, 8, (3), 91-3. (Read full article)

Book Chapter

  1. Steven AC, Belnap D (2008). Cryo-electron microscopy in the era of structural proteomics. 269¿306.
  2. Steven AC, Conway JF, Cheng N, Watts NR, Belnap DM, Harris A, Stahl SJ, Wingfield P (2005). Structure, assembly, and antigenicity of hepatitis B virus capsid proteins. 125-164.
  3. Steven AC, Belnap D (2005). Electron microscopy and image processing: an essential tool for structural analysis of macromolecules. 17.2.1-17.2.39.
  4. Belnap, D (2015). Electron microscopy and image processing: essential tools for structural analysis of macromolecules. 82, 17.2.1-17.2.61.
  5. David M. Belna (2020). Detection of bacteriophages: Electron microscopy and visualisation. 561¿620.

Other

  1. Belnap DM (2013). Journal Cover. J Immunol (191(2)).
  2. Belnap DM (1996). Journal Cover. J Mol Biol (259(2)).
  3. Belnap DM (1999). 40th Anniversary Issue cover. J Mol Biol (293(2)).
  4. Belnap DM (2000). Journal Cover. J Virol (74(7)).
  5. Belnap DM (2011). Journal Cover. J Virol (85(21)).
  6. Belnap DM (2000). Journal Cover. J Virol (74(3)).
  7. Belnap DM (2014). Journal Cover. J Virol (88(20)). American Society for Microbiology.
  8. Belnap D (1996). Cover Figure, Human Papillomaviruses: A Compilation and Analysis of Nucleic Acid and Amino Acid Sequences, Los Alamos National Laboratory, Los Alamos, New Mexico, http://hpv-web.lanl.gov/.
  9. Belnap D (1997). Cryo-Reconstruction Flow Chart, in Baker, T. S. & Johnson, J. E. "Principles of Virus Structure Determination". 49,73.
  10. Belnap D (1999). Fig. 10 of Baker, T. S., Olson, N. H., & Fuller, S. D. "Principles of Virus Structure Determination". 63, 862-922.
  11. Belnap D (1998). Journal Cover. 123(3), 3.
  12. Belnap D (2000). Poliovirus cell-entry diagram. 7(4), 31.
  13. Belnap D (2011). Journal Cover. 411(1), 1.
  14. Belnap D (2014). Poliovirus picture for book on polio eradication: Sarah Gibbard Cook, Rotary and the Gift of a Polio-Free World: Vol 1. Making the Promise.
  15. Belnap D (2015). The theory of evolution is compatible with both belief and unbelief in a supreme being. 16, 261-281.
  16. Belnap D (2016). The theory of evolution is compatible with both belief and unbelief in a supreme being. 369-392.
  17. Belnap D (2016). Questions and comments about evolution. 393-409.
  18. Momont C, Dang HV, Zatta F, Hauser K, Wang C, di Iulio J, Minola A, Czudnochowski N, De Marco A, Branch K, Donermeyer D, Vyas S, Chen A, Ferri E, Guarino B, Powell AE, Spreafico R, Yim SS, Balce DR, Bartha I, Meury M, Croll TI, Belnap DM, Schmid MA, Schaiff WT, Miller JL, Cameroni E, Telenti A, Virgin HW, Rosen LE, Purcell LA, Lanzavecchia A, Snell G, Corti D, Pizzuto M (2023). Author Correction: A pan-influenza antibody inhibiting neuraminidase via receptor mimicry. Nature, 619(7970), E50. (Read full article)

Video/Film/CD/Web/Podcast

  1. Belnap D (2008). Poliovirus pictures for "Stamping Out Polio".
  2. Belnap D (2014). Poliovirus picture for documentary on poliomyelitis, The Battle to Beat Polio.
  3. Belnap DM, Peek LW, Wells (2014). Radio Interview, Cool Science Radio, August 28, 2014.
  4. Markham D, Markham L, Belnap (2017). "What's Inside a Microscope?".