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Full-Text Articles in Molecular Biology

The Release Of Calcium In Bacillus Anthracis Pathogenicity Methods, Natiera Magnuson, Manomita Patra Bhowmik, Maria Elena Reynaga, Ernesto Abel-Santos Apr 2011

The Release Of Calcium In Bacillus Anthracis Pathogenicity Methods, Natiera Magnuson, Manomita Patra Bhowmik, Maria Elena Reynaga, Ernesto Abel-Santos

Festival of Communities: UG Symposium (Posters)

Anthrax infection starts with germination of Bacillus anthracis spores in macrophages. Some bacteria, including B. anthracis, can sporulate in response to environmental stress, such as starvation. During germination, large concentrations of calcium ions are released from the B. anthracis spore. Calcium ions are hydrophilic secondary messengers, and may therefore interfere with detection of the spore by confusing the cell signaling pathways. We investigated calcium release on infected macrophage viability by replacing the calcium stored in B. anthracis spores for other cations via demineralization/remineralization. It was discovered that calcium ions typically out-performed other cations in germination of B. anthracis.


Characterization Of Ips Pini Ipsdienol Dehydrogenase (Idol Dh), Heidi Pak, Claus Tittiger, William Welch Apr 2011

Characterization Of Ips Pini Ipsdienol Dehydrogenase (Idol Dh), Heidi Pak, Claus Tittiger, William Welch

Festival of Communities: UG Symposium (Posters)

Ipsdienol is an important pheromone component for pine engraver beetle, Ips pini. Ipsdienol is a ten carbon monoterpenoid secondary alcohol and ipsdienone is the corresponding ketone. We are characterizing the activity of recombinant IDOL DH produced in Sf9 (insect) cells. The enzyme has a high stereospecificity: (-) ipsdienol was found to be a substrate while (+)-ipsdienol was neither a substrate nor inhibitor. Closely related monoterpenoids, such as nerol, geraniol, and citral, were neither substrates nor inhibitors. Smaller compounds, such as 2-propanol, also failed to act as an inhibitor or substrate. This indicates the binding site of this enzyme is highly …