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X-WR-CALDESC:Events for Institute of Biomedical Engineering (BME)
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DTSTART;TZID=America/Toronto:20260427T100000
DTEND;TZID=America/Toronto:20260427T110000
DTSTAMP:20260416T122617Z
CREATED:20260317T135940Z
LAST-MODIFIED:20260416T122617Z
UID:10000716-1777284000-1777287600@bme.utoronto.ca
SUMMARY:PhD Open Defense - Angelico Raphael Obille
DESCRIPTION:Abstract: While it remains challenging to engineer strong\, biocompatible adhesives that are effective in wet conditions\, many aquatic organisms have evolved strategies to adhere to surfaces underwater. Zebra mussels (Dreissena polymorpha) and quagga mussels (Dreissena bugensis) are freshwater bivalves that use a proteinaceous structure called the byssus to permanently attach to diverse surfaces. Although superficially similar to the marine mussel byssus\, the Dreissenid byssal system evolved in freshwater conditions\, resulting in a unique\, and understudied\, biochemical profile. Understanding the mechanism of byssal adhesion employed by Dreissenids offers potential new insights for the development of bioinspired adhesive materials. The objective of this thesis is to identify and functionally characterize Dreissenid adhesive proteins that directly interface with adherend surfaces. Localization via quantitative proteomics of quagga mussel byssal proteins revealed a set of 20 putatively adhesive footprint proteins. Among these was Dbfp7\, a highly expressed small polymorphic protein that was shown to exhibit adhesive ability in aqueous conditions despite lacking significant amounts of 3\,4-dihydroxyphenylalanine (DOPA). A sequence-reductive approach combined with atomic force nanomechanical mapping and surface-enhanced Raman spectroscopy revealed functional differences between domains of Dbfp7\, revealing sequences that encode adhesive properties. The identification and characterization of Dbfp7 expands the repertoire of known wet adhesive proteins\, furthers our understanding of freshwater bioadhesion\, and provides a new source of inspiration for the development of improved bioinspired wet adhesive materials for applications including medical adhesives. \n\n\n\nMeeting Link: https://utoronto.zoom.us/j/89715577958 \n\n\n\nMeeting ID: 897 1557 7958
URL:https://bme.utoronto.ca/event/phd-open-defense-angelico-raphael-obille/
ATTACH;FMTTYPE=image/png:https://bme.utoronto.ca/wp-content/uploads/2026/03/Angelico-Obille-Defense.png
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DTSTART;TZID=America/Toronto:20260428T110000
DTEND;TZID=America/Toronto:20260428T120000
DTSTAMP:20260416T134528Z
CREATED:20260409T134052Z
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UID:10000718-1777374000-1777377600@bme.utoronto.ca
SUMMARY:BME Faculty Member Search- Stephanie Gaglione- Decoding and engineering T cell recognition at scale
DESCRIPTION:T cells respond to specific antigens in cancer\, infection\, and autoimmunity\, yet these interactions remain among the least predictable in biology. Decoding this specificity is key to designing targeted immunotherapies\, but existing technologies cannot link the vast diversity of T cell receptors (TCRs) and antigens. Addressing this major challenge\, I introduce tools to sensitively map TCRs to antigens at scale and apply them to pinpoint disease-relevant T cells in autoimmunity and cancer. Sequencing of patient samples generates large-scale data on immune receptor sequences and cell states but little information on antigen specificity. I developed an inexpensive approach to reconstruct TCRs from sequence data alone and functionally test them against hundreds of antigens simultaneously. Using this pipeline\, I precisely identified autoreactive T cells in vitiligo and found transcriptomic signatures similar to skin-reactive T cells in melanoma. Extending this work\, I developed a platform capable of even larger screens—millions of TCRs against hundreds of antigens at once. My research group will build on these tools to decode and reprogram antigen-specific T cells\, engineering the next generation of targeted immunotherapies.
URL:https://bme.utoronto.ca/event/bme-faculty-member-search-stephanie-gaglione/
LOCATION:Health Sciences Building\, Room 108\, 155 College St\, Toronto\, ON\, M5S 3E3\, Canada
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