One of the key components to vertebrate survival is the innate ability to produce interferons (IFN). Type 1 IFN are regulatory proteins expressed in response to infection caused by invading viruses. The synthesis of these cytokines is upregulated through several different cellular pathways. For instance, the RIG‐I pathway detects foreign viral RNA enabling the CARD domains of RIG‐I to be ubiquitinized by the enzyme, TRIM25. This initiates a signaling cascade which ultimately results in the expression of IFN. Once produced, IFN are released from the infected cell and bind to IFN‐alpha/beta receptors on the epithelial cells of the respiratory system. This consequently produces antiviral cytokines which degrade viral RNA. In defense to this mechanism, Influenza A virus carries an NS1 gene that has been shown to compromise the regulation of IFN. NS1 binds to TRIM25, preventing the enzyme from ubiquitinating RIG‐I and ultimately inhibiting cytokine production. NS1, although not necessary for construction of the virus itself, compromises the innate immune system, resulting in the flu. The E.E. Waddell SMART Team (Students Modeling A Research Topic), in collaboration with MSOE, has built accurate models of IFN and NS1 using 3D printing technology. Supported by a grant from NIH‐NCRR‐SEPA.
Meningitis is an inflammation of the meninges, membranes that cover the brain and spinal cord. It can be caused by several pathogenic agents existing in the nasopharynx region of humans. The gram‐negative bacterium, Neisseria meningitidis, confers pathogenicity when it sheds its capsule, crosses the epithelium layer and enters the bloodstream via transcytosis. Upon entry, the bacterium reforms its capsule and modulates its adhesins, such as pili and opacity proteins (Opc) to avoid the hosts' immune response and to adhere to epithelial cells of the meninges. While en route to the meninges, lipopolysaccarides adhesins may induce septicemia by causing toxic damage to cells. Upon arrival to its host meninges, it wreaks havoc by utilizing basic residues on the crevice of its OpcA protein to increase interaction with polysaccarides and heparin, a receptor on the host's meninges. This bond forms a bridge enabling OpcA to bind with fibronectin inducing interaction with integrins, aiding with cellular adhesion to the extracellular matrix during transcytosis. By understanding the structure of OpcA we can inhibit the interaction between N.meningitis and host cells with a vaccine that can potentially prevent meningitis. The E.E. Waddell SMART (Students Modeling A Research Topic) Team along with MSOE built accurate models of OpcA, heparin, and fibronectin using 3D printing. Supported by a grant from NIH‐NCRR‐SEPA
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