About

Daniel DiMaio, MD, PhD, is the Principal Investigator of the DiMaio Lab at Yale School of Medicine. He holds the distinguished title of Waldemar Von Zedtwitz Professor of Genetics and also serves as a Professor of Molecular Biophysics and Biochemistry and of Therapeutic Radiology. The lab members page lists him as the leading faculty member, indicating his central role in guiding research efforts within the lab. However, the provided page text does not include detailed information about his specific research focus, background, or key scientific contributions beyond his academic titles and leadership position within the lab.

Research topics

• Biology
• Cell biology
• Biochemistry
• Virology
• Chemistry
• Political Science
• Physics
• Biophysics
• Immunology
• Medicine
• Pathology
• Genetics

Selected publications

• Cargo-Adaptor Cooperation Programs Retromer Coat Architecture

  bioRxiv (Cold Spring Harbor Laboratory) · 2026-05-07

  articleOpen access

  Retromer drives endosomal cargo retrieval in combination with sorting nexin (SNX) adaptors, but how adaptor-cargo combinations specify coat architecture remains unclear. We identify sorting nexin 12 (SNX12) as the retromer adaptor required for human papillomavirus 16 (HPV16) infection and show that the viral L2 capsid protein tail directly engages SNX12-retromer complexes to trigger membrane tubulation. The crystal structure reveals a conserved cargo-recognition mode, whereas cryo-electron tomography of reconstituted assemblies shows retromer arches organized into two lattice configurations stabilized by membrane-proximal interfaces. These lattices assemble as multi-start helices and accommodate curvature through hinge-like motions between arches. These findings establish cargo and adaptor identity as co-determinants of retromer coat architecture, revealing retromer as a programmable system capable of generating route-specific transport carriers.

  PublisherDOI

• Abstract 3985 Cryo-electron microscopy and AlphaFold modeling reveal multiple conformations of the human papillomavirus L2 protein in the viral capsid

  Journal of Biological Chemistry · 2026-05-01

  articleOpen accessSenior author
  PublisherDOI

• Golgi-associated nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection

  bioRxiv (Cold Spring Harbor Laboratory) · 2025-01-13 · 1 citations

  preprintOpen access

  Abstract During human papillomavirus (HPV) entry, the virus exploits COPI-dependent retrograde transport to cross the trans-Golgi network and Golgi stacks before reaching the nucleus to cause infection. How HPV enters the nucleus after exiting the Golgi is unclear, although mitotic nuclear envelop breakdown (NEB) appears important. Here we show that importin-7 (IPO7), a nuclear pore import receptor, associates with the Golgi and promotes HPV infection. Upon IPO7 knockdown, HPV infection is inhibited and the virus accumulates in the Golgi but does not enter the nucleus, demonstrating that IPO7 promotes Golgi-to-nucleus transport of HPV. We further reveal that the C-terminus of HPV capsid protein L2, which is thought to contain overlapping nuclear localization and cell-penetrating peptide sequences, binds directly to IPO7 in a step that requires COPI-dependent virus trafficking. Together these data identify a role of an importin in HPV infection, raising the possibility that the canonical nuclear pore import machinery plays an unanticipated role in NEB-dependent nuclear entry. Teaser HPV, a cancer-causing human pathogen, exploits the Golgi-associated nuclear import receptor IPO7 for Golgi-to-nucleus trafficking to promote infection.

  PublisherOA PDFDOI

• γ-secretase facilitates retromer-mediated retrograde transport

  Journal of Cell Science · 2025-01-27 · 1 citations

  articleOpen accessSenior author

  Retromer mediates retrograde transport of protein cargoes from endosomes to the trans-Golgi network (TGN). γ-secretase is a protease that cleaves the transmembrane domain of its target proteins. Although retromer can form a stable complex with γ-secretase, the functional consequences of this interaction are not known. Here, we report that retromer-mediated retrograde protein trafficking in cultured human epithelial cells is impaired by the γ-secretase inhibitor XXI or by knockout of PS1 (also known as PSEN1), the catalytic subunit of γ-secretase. These treatments inhibited endosome-to-TGN trafficking of retromer-dependent retrograde cellular cargoes, divalent metal transporter 1 isoform II, cation-independent mannose-6-phosphate receptor and shiga toxin, whereas trafficking of retromer-independent cargoes, cholera toxin and a mutant CIMPR unable to bind retromer was not affected. Moreover, we found that γ-secretase associates with retromer cargoes even in the absence of retromer. XXI treatment and PS1 knockout did not inhibit the ability of retromer or γ-secretase to associate with cargo and did not affect the expression of retromer subunits or Rab7-GTP, which regulates retromer-cargo interaction. These results imply that the γ-secretase-retromer interaction facilitates retromer-mediated retrograde trafficking of cellular transmembrane proteins.

  PublisherOA PDFDOI

• The nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection

  Science Advances · 2025-10-22

  articleOpen access

  During human papillomavirus (HPV) entry, the virus exploits COPI-dependent retrograde transport to cross the Golgi apparatus before reaching the nucleus to cause infection. How HPV enters the nucleus after exiting the Golgi is unclear, although mitotic nuclear envelope breakdown (NEB) appears important. Here, we show that importin-7 (IPO7), a nuclear pore import receptor, is present at the Golgi and promotes HPV infection. IPO7 knockdown inhibits infection and causes HPV to accumulate in the Golgi without reaching mitotic chromosomes, demonstrating that IPO7 promotes Golgi-to-nucleus transport of HPV. Golgi-to-nucleus transport of a cellular cargo also requires IPO7, suggesting that HPV hijacks a preexisting pathway for nuclear entry. Furthermore, the C-terminal nuclear localization sequence of HPV L2 protein, which overlaps its cell-penetrating peptide sequence, binds IPO7 directly in a COPI-dependent virus trafficking step. Together, these data identify a role for an importin in HPV infection and suggest that the canonical nuclear pore import machinery plays an unanticipated role in NEB-dependent nuclear entry.

  PublisherDOI

• A modular vaccine platform for optimized lipid nanoparticle mRNA immunogenicity

  Nature Biomedical Engineering · 2025-08-25 · 4 citations

  article
  PublisherDOI

• The BICD2 dynein cargo adaptor binds to the HPV16 L2 capsid protein and promotes HPV infection

  PLoS Pathogens · 2024-06-03 · 11 citations

  articleOpen accessCorresponding

  During entry, human papillomavirus (HPV) traffics from the endosome to the trans Golgi network (TGN) and Golgi and then the nucleus to cause infection. Although dynein is thought to play a role in HPV infection, how this host motor recruits the virus to support infection and which entry step(s) requires dynein are unclear. Here we show that the dynein cargo adaptor BICD2 binds to the HPV L2 capsid protein during entry, recruiting HPV to dynein for transport of the virus along the endosome-TGN/Golgi axis to promote infection. In the absence of BICD2 function, HPV accumulates in the endosome and TGN and infection is inhibited. Cell-based and in vitro binding studies identified a short segment near the C-terminus of L2 that can directly interact with BICD2. Our results reveal the molecular basis by which the dynein motor captures HPV to promote infection and identify this virus as a novel cargo of the BICD2 dynein adaptor.

  PublisherOA PDFDOI

• The Genetics of Bovine Papillomavirus Type 1

  2024-12-09

  book-chapter1st authorCorresponding

  Bovine papillomavirus type 1 (BPV1) is a small DNA virus that induces skin fibropapillomas in cattle. BPV1 also induces the formation of fibroblastic tumors in laboratory animals and readily causes stable transformation of cultured bovine cells and cells from heterologous species. BPV1-transformed cells express altered growth characteristics including, in some cases, the ability to form tumors. These cells contain the viral DNA as a stable nuclear plasmid, but no progeny viruses are produced. This nonproductive interaction of BPV1 with cultured cells has been studied widely as an example of tumorigenic transformation and as an analogue of the interaction of the virus with dermal fibroblasts and basal epithelial cells in a fibropapilloma.

  PublisherDOI

• Virology—the path forward

  Journal of Virology · 2024-01-03 · 9 citations

  articleOpen access

  In the United States (US), biosafety and biosecurity oversight of research on viruses is being reappraised. Safety in virology research is paramount and oversight frameworks should be reviewed periodically. Changes should be made with care, however, to avoid impeding science that is essential for rapidly reducing and responding to pandemic threats as well as addressing more common challenges caused by infectious diseases. Decades of research uniquely positioned the US to be able to respond to the COVID-19 crisis with astounding speed, delivering life-saving vaccines within a year of identifying the virus. We should embolden and empower this strength, which is a vital part of protecting the health, economy, and security of US citizens. Herein, we offer our perspectives on priorities for revised rules governing virology research in the US.

  PublisherOA PDFDOI

• Correction for Rasmussen et al., “Virology—the path forward”

  Journal of Virology · 2024-02-09 · 4 citations

  erratumOpen access

  7: "elevating SARS-CoV-1 to a select agent in 2009" should read "elevating SARS-CoV-1 to a select agent in 2012."The CDC proposed adding SARS-CoV-1 to the Select Agent registry in a federal notice on 13 July 2009 (https://www.federalregister.gov/documents/2009/07/13/E9-16536/posses sion-use-and-transfer-of-select-agents-and-toxins-proposed-addition-of-sars-associ ated).This notice of proposed rulemaking explicitly states that compliance with the proposed amendment would require anyone possessing SARS-CoV-1 to obtain current or amended registration with the HHS Select Agent Program and acknowledged that registration is a time-consuming and potentially costly process.Contemporaneous sources demonstrate that the research impact was anticipated in 2009 (https://absa.org/wpcontent/uploads/2017/01/090911DHHS_SARS_Select_Agent_Comments.pdf and https:// www.cidrap.umn.edu/sars/cdc-proposes-list-sars-virus-select-agent) and had already had a negative impact on SARS-CoV-1 research (S.

  PublisherOA PDFDOI

Recent grants

• Mechanisms of human papillomavirus entry

  NIH · $5.9M · 2020–2027

• Molecular Basis of Cancer Virus Replication, Transformation, and Innate Defense

  NIH · $62.7M · 2020–2021

• Retrograde TGN/Golgi transport and nuclear targeting of HPV during entry

  NIH · $3.5M · 2020–2031

• Predoctoral Training Program in Virology

  NIH · $3.2M · 2003–2025

• Role of Retromer-mediated Retrograde Transport in HPV Entry

  NIH · $3.1M · 2013–2024

Frequent coauthors

• Edward C. Goodwin

  Bioarray Genetics (United States)

  34 shared

• Walter J. Atwood

  Providence College

  32 shared

• Anne P. B. Edwards

  Yale University

  26 shared

• Lisa M. Petti

  Yale University

  21 shared

• Donald M. Engelman

  Yale University

  20 shared

• Char‐Chang Lai

  19 shared

• Terence S. Dermody

  University of Pittsburgh

  18 shared

• Joan A. Steitz

  Yale University

  18 shared

Labs

• DiMaio LabPI

  Name Years in Lab Current Position

Education

• Ph.D., Genetics

  Yale University

  1990

• M.D.

  Yale University School of Medicine

  1985

• B.S., Biology

  University of California, San Diego

  1981