Gonzalo González-Del Pino

He/They

Assistant Professor

Faculty
Headshot of Gonzo González-Del Pino standing outside wearing a red bowtie
Contact
Email
Email
Phone
Location
LSL N375

Focus

Using structure-based methods to understand host entry and oncogenesis in gammaherpesviruses

Background and Training

PhD: Harvard University

Postdoctoral training: Tufts University School of Medicine

Research Summary

Human herpesviruses, categorized into the alpha, beta, and gamma subfamilies, are highly successful enveloped viruses that infect nearly all humans for life1. There is no cure for any herpesvirus infection, and treatment and vaccination options remain woefully limited2. Identifying novel therapeutic targets requires a deeper understanding of herpesvirus biology. The goal of my group is to determine how disease-specific protein machines operate by mapping their conformational pathways and function-relevant complexes using novel biophysical approaches. Specifically, we study the proteins and complexes involved in host entry and oncogenic transformation by the cancer-causing gammaherpesviruses, Epstein-Barr Virus and Kaposi Sarcoma-Associated Herpesvirus. Overall, work in my lab will identify novel therapeutic targets and develop new methodologies for studying protein machines in their disease-relevant complexes and conformations.

The two questions we aim to answer:
1.    How do gammaherpesviruses enter their host cells?
2.    How do these viruses transform their host cells into cancer?

Series of figures titled "Structure-based mechanistic studies of gammaherpesvirus infection and oncogenesis"

References
1. N., F., Bernard, 1950-, K., David M. (David Mahan), & M., H., Peter. Fields virology. (2013).
2. Poole, C. L. & James, S. H. Antiviral Therapies for Herpesviruses: Current Agents and New Directions. Clin. Ther. 40, 1282–1298 (2018).

Publications

Preprint 

  • Gonzalez-Del Pino, G.L.*, Walsh, R.M. Jr.*, Cairns, T.M., Atanasiu, D., Saw, W.T., Cohen, G.H., Heldwein, E.E. (2024). Allosteric mechanism of membrane fusion activation in a herpesvirus. bioRxiv 2024.09.20.610514. https://doi.org/10.1101/2024.09.20.610514.

Published

  • Gonzalez-Del Pino, G.L., Heldwein, E.E. (2026). Pre-assembled complexes and allosteric effects: parallels between eukaryotic phosphorylation cascades and membrane fusion during herpesviral entry. J Virol 0:e01704-24. https://doi.org/10.1128/jvi.01704-24
  • McNellis, M.*, Gonzalez-Del Pino, G.L.*, Forster, E.R., Stoica, A.I., Serrano, J.A., Heldwein, E.E., Shen A. (2025). Homo- and hetero-dimerization of Clostridiodes difficile Csp proteins regulates germination in response to bile salts and co-germinants. PLoS Bio. In press.
  • Gonzalez-Del Pino, G.L., and Rokop, M.E. (2024). Diving into research without wading through content: A skills-based cell biology course emphasizing the unknown. Biochem Mol Biol Educ. https://doi.org/10.1002/bmb.21858.
  • Draganova, E.B., Wang, H., Wu, M., Liao, S., Vu, A., Gonzalez-Del Pino, G.L., Zhou, Z.H., Roller, R.J., Heldwein, E.E. (2024) Structural characterization of a universal suppressor mutation in the HSV-1 nuclear egress complex oligomeric lattice. Biophysical Journal 123 (3), 312a.
  • Draganova, E.B., Wang, H., Wu, M., Liao, S., Vu, A., Gonzalez-Del Pino, G.L., Zhou, Z.H., Roller, R.J., Heldwein, E.E. (2024). The universal suppressor mutation in the HSV-1 nuclear egress complex restores membrane budding defects by stabilizing the oligomeric lattice. PLoS Pathogen 20 (1), e1011936.
  • Tkacik, E.*, Li, K.*, Gonzalez-Del Pino, G.L., Ha, B.H., Vinals, J., Park, E., Beyett, T.S., and Eck, M.J. (2023). Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib. J. Biol. Chem. 299, 104634. 10.1016/j.jbc.2023.104634.
  • Gonzalez-Del Pino, G.L., and Heldwein, E.E. (2022). Well Put Together—A Guide to Accessorizing with the Herpesvirus gH/gL Complexes. Viruses 14, 296. 10.3390/v14020296.
  • Gonzalez-Del Pino, G.L.*, Li, K.*, Park, E., Schmoker, A.M., Ha, B.H., and Eck, M.J. (2021). Allosteric MEK inhibitors act on BRAF/MEK complexes to block MEK activation. Proc National Acad Sci 118, e2107207118. 10.1073/pnas.2107207118.
  • Park, E., Rawson, S., Li, K., Kim, B.W., Ficarro, S.B., Gonzalez-Del Pino, G.L., Sharif, H., Marto, J.A., Jeon, H., and Eck, M.J. (2019). Architecture of autoinhibited and active BRAF-MEK1-14-3-3 complexes. Nature 575, 545–550. 10.1038/s41586-019-1660-y.
  • Cai, W.*, Sakaguchi, M.*, Kleinridders, A., Gonzalez-Del Pino, G.L., Dreyfuss, J.M., O’Neill, B.T., Ramirez, A.K., Pan, H., Winnay, J.N., Boucher, J., et al. (2017). Domain-dependent effects of insulin and IGF-1 receptors on signalling and gene expression. Nat. Commun. 8, 14892. 10.1038/ncomms14892.