Illuminating Substrate-Recognizing Mechanisms in the Haemophilus influenzae Immunoglobulin A1 Protease

Immunoglobulin A1 proteases (IgAPs) are biological catalysts (enzymes) produced by many pathogens of the human respiratory tract. Their ability to infect these tissues heavily relies on IgAPs, so much so that those unable to produce a functional enzyme are unable to cause disease. As blocking IgAP activity theoretically halts the infection process, IgAPs are a worthwhile target for drug-developing research aimed at finding new respiratory infection treatments. If successful, these new therapeutics will provide a much-needed alternative to traditional antibiotics, especially important considering the foreseeable consequences of antibiotic-resistant bacteria. Unfortunately, this is still in the distant future. Scientists currently do not fully understand the mechanisms guiding IgAP function, information needed to increase the chances of developing a successful clinical drug. I will bridge this gap by using cryogenic electron microscopy to illuminate molecular interactions between a specific IgAP and the molecule it naturally acts on. This will provide atomic-level information that will guide future research on new treatment options against respiratory infections.

Faculty Supervisor:

Todd Holyoak

Student:

Partner:

University of Colorado Denver

Discipline:

Life Sciences

Sector:

Education

University:

University of Waterloo

Program: