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Home > TJU > Student Works > ALPHA_OMEGA_ALPHA_RESEARCH_SYMPOSIUM > AOA_RESEARCH_SYMPOSIUM_POSTERS

Alpha Omega Alpha Research Symposium Posters

 

There is an annual poster session hosted by the AOA to highlight research endeavors of SKMC students. This day offers an opportunity for students to network with faculty and features a physician keynote speaker. The event also awards student investigators who have displayed significant research findings.

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  • Broad Efficacy of a Computationally Designed ACE2 Decoy Against SARS-CoV-2 Omicron Variants and Related Viruses In Vitro and In Vivo by Brandon Havranek, Graeme W. Lindsey, Yusuke Higuchi, Yumi Itoh, Tatsuya Suzuki, Toru Okamoto, Atsushi Hoshino, Erik Procko, and Shahidul M. Islam

    Broad Efficacy of a Computationally Designed ACE2 Decoy Against SARS-CoV-2 Omicron Variants and Related Viruses In Vitro and In Vivo

    Brandon Havranek, Graeme W. Lindsey, Yusuke Higuchi, Yumi Itoh, Tatsuya Suzuki, Toru Okamoto, Atsushi Hoshino, Erik Procko, and Shahidul M. Islam

    Background: The SARS-CoV-2 omicron variant (B.1.1.529) and its sublineages are currently the dominant variants in the United States accounting for 100% of COVID-19 cases. Problem: The S protein receptor-binding domain (RBD), located in the S1 subunit of the S protein, binds the human angiotensin-converting enzyme 2 (hACE2) leading to S1 shedding and proteolytic processing of S2 that is important for membrane fusion and release of viral RNA. Various neutralizing therapeutics including protein minibinders, peptides, monoclonal antibodies, and nanobodies have been developed to block the critical interaction between the RBD and hACE2. However, these therapeutics are often developed against the S protein of wildtype or a specific variant of SARSCoV- 2, making them highly susceptible to mutational escape.1 Solution: A strategy employed by our group includes using sACE2 (soluble dimeric ACE2 that contains both the protease and dimerization domains) with enhanced S RBD affinity to outcompete native ACE2 expressed on host cells, acting as a ‘decoy’ to block the interaction between the RBD and hACE2 (Figure 1). sACE2 has moderate affinity for the S protein (~20 nM)2. Therefore, sACE2 must be engineered (by introducing affinity enhancing mutations) to bind with tighter affinity to outcompete membrane bound ACE2-S interaction and rival the potency of mAbs. These sACE2 derivatives maintain close similarity to the native ACE2 receptor making them extremely resistant to virus escape. Any mutation in the RBD that limits binding to the sACE2 derivative will likely have reduced binding towards native ACE2 receptors potentially making the virus unfit to propagate.

  • Evaluation of Autofluorescence Technology in the Identification of Tissue Types in Anterior Neck Surgery by Natalie M. Perlov; Elliott Sina; Sruti Tekumalla; Annie Moroco, MD; and Elizabeth Cottrill, MD

    Evaluation of Autofluorescence Technology in the Identification of Tissue Types in Anterior Neck Surgery

    Natalie M. Perlov; Elliott Sina; Sruti Tekumalla; Annie Moroco, MD; and Elizabeth Cottrill, MD

    Background

    • Iatrogenic parathyroidectomy and hypocalcemia are potential risks of central neck surgery1
    • Resected parathyroid tissue may be reimplanted if identified quickly, mitigating risk of hypocalcemia2
    • Current practices of identifying and preserving parathyroids, such as frozen specimens, may incur significant costs in time and expense
    • Autofluorescence (AF) technology takes baseline AF readings from healthy thyroid tissue and compares to other tissues in the neck
    • There is limited data on AF profiles of all tissue types in the central neck (thyroid, thymus, benign vs. malignant lymph nodes, adipose tissue)

    Preliminary Outcomes

    • (1) Investigate the impact of AF on iatrogenic hypoparathyroidism
    • (2) Assess new AF profiles for different tissue types in the anterior neck

 
 
 

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