| Cory
Hill
Mentor:
Dr. Champion Deivanayagam
Internship: Center for Biophysical Sciences
and Engineering, University of Alabama
Title: Expressing and Purifying Proteins
Utilizing Various Growth Methods
Infectious bacteria, such as Listeria monocytogenes,
are composed of a thick cell wall dotted with surface proteins
designed to interact specifically with human cells as a first
step towards establishing infections. These pathogens anchor
themselves to the cell membrane of our body’s cells
and Sortase is a gram-positive bacterial enzyme that aids
in the anchoring of bacteria to the cell wall of human cells.
Without this outer weaponry, gram-positive bacteria could
not invade people’s throats, skin and other susceptible
tissues. Sortase works by activating a five-amino acid tag
present on many of the proteins localized on the bacterial
cell wall, abbreviated LPXTG, where L is Leucine, P is Proline,
X is any amino acid, T is Threonine, and G is Glutamine. It
is this tag that is hooked directly into the cell wall of
human cells, allowing infection. Sortase effectively cleaves
the LPXTG motif near the middle before linking the remainder
of the protein to the cell wall. Hypothetically speaking,
if the cleaving and “sorting” actions of sortase
could be restricted, then scientists would have a modern weapon
in the fight against bacterial infection. We sought out to
purify sortase in order to make crystals for research. From
these crystals, researchers will attempt to produce a working
model of a sortase inhibitor. This inhibitor would revolutionize
the way in which we view bacterial anchoring. A fully-functional
working model could lead to the global eradication of gram-positive
bacterial infections, including Diphtheria, Listeria, Tuberculosis,
Scarlet Fever, and Leprosy.
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