Contact

  • Academic
    phamd@stanford.edu
    University - Student Department: BioPhysics Position: Graduate

All Publications

  • Oriented Multivalent Display Drives Consistent Serum Immunodominance to the Ebola Virus Glycoprotein. ACS central science Zheng, C., Rubio, A. A., Vasquez, S., Pham, D., Pan, Z., Barnes, C. O., Kim, P. S. 2026; 12 (1): 100-110

    Abstract

    Despite the vast diversity of B cell repertoires, serum antibody responses during viral infection often focus on a limited set of epitopesa phenomenon known as immunodominance. This inherent bias establishes a hierarchy of epitope responses, which often facilitates viral immune evasion and presents a major challenge for universal vaccine design. It remains unclear whether serum immunodominance is primarily driven by antigen-intrinsic properties or by the spatial constraints imposed by virion-bound antigen presentation. Here, using Ebola virus glycoprotein (GP) as a model system, we found that trimeric GP elicited varied epitope hierarchies between individual animals during primary immunization. In contrast, multivalent GP presentation on either a vesicular stomatitis virus or ferritin nanoparticlesin the native orientation found on the Ebola viruselicited highly consistent and more refined epitope hierarchies across multiple mice and guinea pigs. These findings reveal a key role of oriented multivalent presentation in shaping serum immunodominance. The striking consistency of epitope hierarchy among individuals suggests that oriented multivalent presentation may promote more uniform immune protection at the population level, beyond increasing the magnitude of antibody binding and neutralizing responses.

    View details for DOI 10.1021/acscentsci.5c01886

    View details for PubMedID 41625225

    View details for PubMedCentralID PMC12856675

  • Oriented Multivalent Display Drives Consistent Serum Immunodominance to the Ebola Virus Glycoprotein ACS CENTRAL SCIENCE Zheng, C., Rubio, A. A., Vasquez, S., Pham, D., Pan, Z., Barnes, C. O., Kim, P. S. 2026

    View details for DOI 10.1021/acscentsci.5c01886

    View details for Web of Science ID 001659224400001

  • A broad antibody with enhanced HIV-1 neutralization via bispecific antibody-mediated prepositioning. Nature communications Kim, S., Radford, C. E., Xu, D., Zhong, J., Do, J., Pham, D. M., Travisano, K. A., Filsinger Interrante, M. V., Bruun, T. U., Rezek, V., Wilder, B., Palomares, M., Seaman, M. S., Kitchen, S. G., Bloom, J. D., Kim, P. S. 2025; 16 (1): 4617

    Abstract

    Antibodies targeting the highly conserved prehairpin intermediate (PHI) of class I viral membrane-fusion proteins are generally weakly neutralizing and are not considered viable therapeutic agents. We previously demonstrated that antibodies targeting the gp41 N-heptad repeat (NHR), which is transiently exposed in the HIV-1 PHI, exhibit enhanced broad neutralization in cells expressing the Fc receptor, FcγRI. To enhance neutralization in cells lacking FcγRI, we here develop a bispecific antibody (bsAb) by fusing an NHR-targeting antibody to an antibody against CD4, the HIV-1 receptor on T cells. The bsAb provides a 5000-fold neutralization enhancement and shows unprecedented neutralization breadth compared to existing broadly neutralizing antibodies. Importantly, the bsAb reduces viral load in HIV-1-infected humanized male mice, and viral envelope sequencing under bsAb pressure revealed an NHR mutation that potentially impairs viral fitness. These findings validate the NHR as a potential HIV-1 therapeutic target, setting the stage for a new class of broadly neutralizing antibodies.

    View details for DOI 10.1038/s41467-025-60035-6

    View details for PubMedID 40383778

    View details for PubMedCentralID 2517140