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)
A V(H)1-69 antibody lineage from an infected Chinese donor potently neutralizes HIV-1 by targeting the V3 glycan supersite
2020; 6 (38)
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
2020; 6 (16): eaaz6225
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