According to the CDC, influenza is the 9th leading cause of death in the US, killing over 50,000 people in 2011. H3N2, an influenza A serotype, is important for current research due to its increasing circulation in humans this season. To combat infections, flu vaccines are administered each year; however, due to continual mutations of the viral proteins, a vaccine offers little protection if the match between it and the dominant circulating strain is poor. Hemagglutinin (HA), the major glycoprotein on the viral surface, binds to host cell sialic acid receptors and initiates viral infection; thus blocking this viral‐host interaction prevents infection. F045–092, a broadly‐neutralizing antibody, targets the receptor binding site of HA and uses remarkable receptor mimicry to recognize all H3 strains from 1968 to 2011. The antibody binds primarily through a long HCDR3 loop that inserts into the HA receptor binding pocket. In addition, the antibody extends its breadth of neutralization using avidity, as the bivalent IgG has higher apparent affinity than the monovalent Fab. This broadly‐neutralizing antibody will potentially enable and inform the development of a pan‐H3 vaccine and small molecule therapeutics. Using 3D printing technology, the Francis Parker SMART (Students Modeling A Research Topic) Team modeled the antibody F045–092 in complex with HA. Supported by a grant from TSRI and UCSD.
Mammals have several mechanisms to maintain homeostasis with respect to body temperature. One such mechanism is brown adipose tissue (BAT), which when activated by cold, functions as a “heater” by converting chemical energy into heat. This reaction is fueled by lipids from both BAT and white adipose tissue, and has the potential to cause significant weight loss. BAT is found in the upper back, neck, between the collarbone and shoulder, and along the spine. Estrogen related receptor gamma (ERRg) is a protein that binds to DNA and regulates genes important for heat production in BAT. The structure of ERRg consists of multiple domains, including a DNA binding domain (DBD) and a regulatory ligand binding domain (LBD). The activity of ERRg is regulated by proteins binding to the LBD; these proteins can either activate gene expression or repress it. It was recently discovered that a cold‐induced protein, Gadd45g, activates ERRg. However, it is unknown how these two proteins interact. Using 3D printing technology, the Francis Parker SMART (Students Modeling A Research Topic) Team modeled the LBD of ERRg and its protein activator Gadd45g. Supported by a grant from the HHMI Pre‐ College Program.
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