Bio


I am a geomicrobiologist and am broadly interested in the connections between protein biochemistry, environmental microbiology, and biogeochemistry. I hail from the surf town of Encinitas near San Diego. I completed my undergraduate studies at the University of Southern California (USC), where I majored in both Biological Sciences and Classical Saxophone Performance. At USC I volunteered in a cellular and molecular neuroscience lab, and it was there that I discovered my fascination with proteins. After graduation, I worked in a vaccine design lab at Scripps Research. This research fostered my growing fascination with protein biochemistry and further exposed me to the realm of microbiology. I have since followed my interests in proteins and microbiology, along with my longstanding passion for climate science, to the field of geomicrobiology. I am currently pursuing a Ph.D. in geomicrobiology at Stanford University in the Earth System Science department.

Honors & Awards


  • Rose Hills Summer Research Fellowship, Rose Hills Foundation (2017)
  • Provost's Undergraduate Research Fellowship, University of Southern California (2017)
  • Renaissance Honors, University of Southern California (2018)

Education & Certifications


  • B.A., University of Southern California, Biological Sciences & Music (2018)

Lab Affiliations


Work Experience


  • Research Assistant II, The Scripps Research Institute (6/1/2018 - 5/1/2020)

    Location

    10550 N Torrey Pines Rd, La Jolla, CA 92037

  • Research Assistant, University of Southern California (9/2016 - 5/2018)

    Location

    Los Angeles, CA 90007

  • Research Assistant, Wildlife Research Institute (5/2016 - 8/2016)

    Location

    18528 Highland Valley Rd, Ramona, CA 92065

All Publications


  • A V(H)1-69 antibody lineage from an infected Chinese donor potently neutralizes HIV-1 by targeting the V3 glycan supersite SCIENCE ADVANCES Kumar, S., Ju, B., Shapero, B., Lin, X., Ren, L., Zhang, L., Li, D., Zhou, Z., Feng, Y., Sou, C., Mann, C. J., Hao, Y., Sarkar, A., Hou, J., Nunnally, C., Hong, K., Wang, S., Ge, X., Su, B., Landais, E., Sok, D., Zwick, M. B., He, L., Zhu, J., Wilson, I. A., Shao, Y. 2020; 6 (38)

    Abstract

    An oligomannose patch around the V3 base of HIV-1 envelope glycoprotein (Env) is recognized by multiple classes of broadly neutralizing antibodies (bNAbs). Here, we investigated the bNAb response to the V3 glycan supersite in an HIV-1-infected Chinese donor by Env-specific single B cell sorting, structural and functional studies, and longitudinal analysis of antibody and virus repertoires. Monoclonal antibodies 438-B11 and 438-D5 were isolated that potently neutralize HIV-1 with moderate breadth, are encoded by the VH1-69 germline gene, and have a disulfide-linked long HCDR3 loop. Crystal structures of Env-bound and unbound antibodies revealed heavy chain-mediated recognition of the glycan supersite with a unique angle of approach and a critical role of the intra-HCDR3 disulfide. The mechanism of viral escape was examined via single-genome amplification/sequencing and glycan mutations around the N332 supersite. Our findings further emphasize the V3 glycan supersite as a prominent target for Env-based vaccine design.

    View details for DOI 10.1126/sciadv.abb1328

    View details for Web of Science ID 000574597200018

    View details for PubMedID 32938661

    View details for PubMedCentralID PMC7494343

  • Proof of concept for rational design of hepatitis C virus E2 core nanoparticle vaccines SCIENCE ADVANCES He, L., Tzarum, N., Lin, X., Shapero, B., Sou, C., Mann, C. J., Stano, A., Zhang, L., Nagy, K., Giang, E., Law, M., Wilson, I. A., Zhu, J. 2020; 6 (16): eaaz6225

    Abstract

    Hepatitis C virus (HCV) envelope glycoproteins E1 and E2 are responsible for cell entry, with E2 being the major target of neutralizing antibodies (NAbs). Here, we present a comprehensive strategy for B cell-based HCV vaccine development through E2 optimization and nanoparticle display. We redesigned variable region 2 in a truncated form (tVR2) on E2 cores derived from genotypes 1a and 6a, resulting in improved stability and antigenicity. Crystal structures of three optimized E2 cores with human cross-genotype NAbs (AR3s) revealed how the modified tVR2 stabilizes E2 without altering key neutralizing epitopes. We then displayed these E2 cores on 24- and 60-meric nanoparticles and achieved substantial yield and purity, as well as enhanced antigenicity. In mice, these nanoparticles elicited more effective NAb responses than soluble E2 cores. Next-generation sequencing (NGS) defined distinct B cell patterns associated with nanoparticle-induced antibody responses, which target the conserved neutralizing epitopes on E2 and cross-neutralize HCV genotypes.

    View details for DOI 10.1126/sciadv.aaz6225

    View details for Web of Science ID 000528276800035

    View details for PubMedID 32494617

    View details for PubMedCentralID PMC7159917