Though the Explorers program introduced me to many fascinating professionals, the lecture delivered by Dr. Katusiime was truly unique in that it paired compelling descriptions of her research with her own educational journey. Unlike many experts however Dr. Katusiime always sincerely appreciated and sought out our participation which made the lecture feel far more personal. Her own education was defined by both resiliency and flexibility. During her time in South Africa she received virtually no financial assistance or support due to her migration status. Though she was not able to enter medical school given these constraints she nevertheless persisted in her education and secured research experience in her PhD program. The way in which she navigated discrimination and financial obstacles was truly inspiring and was communicated very precisely. The frequent questions she asked the group sparked some fascinating discussions and helped me consider the implications her advice would have on my future more deeply. Not only did Dr. Katusiime help us to understand more about what educational pathways are possible, but she also provided the most thorough and precise description of what laboratory research entails I have heard over the course of the program. She mentioned specifically what her days consisted of including bench research, preparing reagents, and departmental meetings. I came away from the talk not only feeling as though I had several concrete steps I could take in my own education, but also that I had acquired a new understanding of what it fundamentally means to be a scientist.
Dr. Katusiime also provided some information about the HIV research she had published and with the current COVID-19 pandemic, research concerning all types of viruses is made all the more important. In the Explorers program I learned more about all levels of the immune system including antibodies, particularly the use of antibody therapies such as checkpoint inhibitor drugs. A study partially authored by Dr. Marzi of the Basic Sciences and Computational Biology Program at Fred Hutch describes a human antibody that could be used against a wide variety of viruses under the subgenus sarbecovirus. The receptor targeted by this antibody is highly conserved and this study also notes that it would be difficult for viruses to be able to mutate so that the receptor is no longer recognized by the antibody. This antibody functions by preventing entry of SARS-CoV-2 into cells by neutralizing the spike proteins which are expressed. More broadly, antibodies are proteins which can bind to other proteins expressed on the surface of cells or viruses to eliminate those microbes, in this case by preventing the virus from entering cells. Experimentally this antigen was tested on Syrian hamsters against the B.1.351 variant and it was determined that the antibody was reasonably effective in preventing and treating infection. Finally this study describes the antigenic site which is targeted by most broadly effective antibodies which paves the way for future research. These promising results are not only applicable to the current COVID-19 pandemic and this antibody might also be utilized for the treatment of other similar zoonotic viruses.
The structure of the SARS-CoV-2 spike protein.
Image from: doi: 10.1126/science.abb2507
Citations:
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., Di Iulio, J., Wang, Z., De Marco, A., Zepeda, S. K., Pinto, D., Liu, Z., Beltramello, M., Bartha, I., Housley, M. P., Lempp, F. A., Rosen, L. E., Dellota, E., Jr, ... Pizzuto, M. S. (2021). Broad sarbecovirus neutralization by a human monoclonal antibody. Nature, 10.1038/s41586-021-03817-4. Advance online publication. https://doi.org/10.1038/s41586-021-03817-4
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C. L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020). Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science (New York, N.Y.), 367(6483), 1260–1263. https://doi.org/10.1126/science.abb2507
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