Authors:

Roberto Angel Garza

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About Paper:

Eastern equine encephalitis virus (EEEV) is an extremely virulent alphavirus. Roughly 5-10% of infected people develop severe encephalitis and the mortality rate among them can be as high as 30%. Additionally, almost 90% of survivors of infection suffer long-term neurological problems. Despite the significant threat that this pathogen represents, there are currently no approved therapeutics or vaccines available for the EEEV virus for human use. Patient-derived neutralizing monoclonal antibodies are promising candidates for potential therapeutics as well as tools to elucidate epitopes on the virus which can then be used for design of vaccines or immunogens. In this report we extend the work on the complex of EEEV with EEEV-373, a potently neutralizing patient-derived antibody. The paper describing this research has been accepted and is about to be published in Nature Communications. The structure of the complex revealed that the antibody displays preferential binding on the virus across the icosahedral twofold. The structure was resolved to 3.8 Å, however, the resolution of the epitope-paratope region reached around 5 Å. Our research is geared toward improving the resolution of the epitope paratope region utilizing the same dataset in cryoSPARC. The main idea behind this is to see if we can resolve the details of the interactions between the CDRs and the residues comprising the epitope. Achieving higher resolution will provide us with as better understanding of this interaction which may aid in development of EEEV-373 as a therapeutic. Additionally, this may also help in designing other inhibitors targeting this particular epitope. Keywords: Eastern Equine Encephalitis Virus (EEEV); EEEV-373; Epitope- Paratope; cryoSPARC

Source:

Purdue University / 2025

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Co-authors:

Roberto Angel Garza