Date of Award


Document Type

Restricted Thesis

Terms of Use

© 2022 Emma J. Parker Miller. All rights reserved. Access to this work is restricted to users within the Swarthmore College network and may only be used for non-commercial, educational, and research purposes. Sharing with users outside of the Swarthmore College network is expressly prohibited. For all other uses, including reproduction and distribution, please contact the copyright holder.

Degree Name

Bachelor of Arts


Chemistry & Biochemistry

First Advisor

Daniela Fera


Elicitation of broadly neutralizing antibodies (bnAbs) is a goal of vaccine design as a strategy for targeting highly divergent strains of HIV-1. However, design of an effective vaccine to elicit bnAbs will require an understanding of the co-evolution process between the virus, bnAbs, and cooperating antibody lineages in a host. DH272 is a cooperating antibody that exerted pressure on HIV to evolve in such a way that it became sensitive to the DH270 bnAb lineage from an HIV-1 infected donor, called CH848. In this study, we present data characterizing an antibody fragment, called DH272.2, that is related to DH272, and its interactions with the transmitted founder (TF) HIV-1 Env from patient CH848 to understand how DH272 facilitated the development of DH270 bnAbs. Data suggest that the antibody CDRH3 loop, and the Env V1/V2 and V3 loops are critical for interaction. However, further work is needed to develop a more complete model of this interaction and a rationale for the mechanism through which DH272 acts as a cooperating antibody.