Date of Completion
Greg Huber; Patrick McKenna; William Abikoff
Bioinformatics | Molecular Biology
The flu virus was investigated to find a common recognition domain to which an antibody against human-infected viruses can bind. If such a target site is structurally and electrostaticly conserved or invariant, only a single antibody would be required to attack the virus in all cases. The sequence of one of the viral surface proteins contains 24 amino acids that do not vary through mutation. However, these amino acids are neither contiguous in sequence or in space, and the ones that are associated with each other are not readily accessible to an antibody. They do provide a first impression of which regions of the surface have the potential to serve as a common recognition site, and a broader search requiring more computational power may reveal a region of the protein surface that is structurally stable across all strains and is available for binding to a soluble antibody.
Norton, Scott S., "Numerical assessment of sequence conservation in flu-virus hemagglutinin" (2014). Honors Scholar Theses. 365.