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Full-Text Articles in Life Sciences
Structure-Guided Molecular Grafting Of A Complex Broadly Neutralizing Viral Epitope, G. Bajic, M. J. Maron, T. M. Caradonna, M. Tian, Adam Mermelstein , '21, Daniela Fera, G. Kelsoe, M. Kuraoka, A. G. Schmidt
Structure-Guided Molecular Grafting Of A Complex Broadly Neutralizing Viral Epitope, G. Bajic, M. J. Maron, T. M. Caradonna, M. Tian, Adam Mermelstein , '21, Daniela Fera, G. Kelsoe, M. Kuraoka, A. G. Schmidt
Chemistry & Biochemistry Faculty Works
Antigenic variation and viral evolution have thwarted traditional influenza vaccination strategies. The broad protection afforded by a “universal” influenza vaccine may come from immunogens that elicit humoral immune responses targeting conserved epitopes on the viral hemagglutinin (HA), such as the receptor-binding site (RBS). Here, we engineered candidate immunogens that use noncirculating, avian influenza HAs as molecular scaffolds to present the broadly neutralizing RBS epitope from historical, circulating H1 influenzas. These “resurfaced” HAs (rsHAs) remove epitopes potentially targeted by strain-specific responses in immune-experienced individuals. Through structure-guided optimization, we improved two antigenically different scaffolds to bind a diverse panel of pan-H1 and …
The Effects Of Framework Mutations At The Variable Domain Interface On Antibody Affinity Maturation In An Hiv-1 Broadly Neutralizing Antibody Lineage, Jeffrey O. Zhou , '19, Hussain A. Zaidi , '22, Therese Ton , '19, Daniela Fera
The Effects Of Framework Mutations At The Variable Domain Interface On Antibody Affinity Maturation In An Hiv-1 Broadly Neutralizing Antibody Lineage, Jeffrey O. Zhou , '19, Hussain A. Zaidi , '22, Therese Ton , '19, Daniela Fera
Chemistry & Biochemistry Faculty Works
Understanding affinity maturation of antibodies that can target many variants of HIV-1 is important for vaccine development. While the antigen-binding site of antibodies is known to mutate throughout the co-evolution of antibodies and viruses in infected individuals, the roles of the mutations in the antibody framework region are not well understood. Throughout affinity maturation, the CH103 broadly neutralizing antibody lineage, from an individual designated CH505, altered the orientation of one of its antibody variable domains. The change in orientation was a response to insertions in the variable loop 5 (V5) of the HIV envelope. In this study, we generated CH103 …