Publications by authors named "N Punja"

There has been a steady increase in illness incidence of Vibrio parahaemolyticus (Vp). The majority of illnesses are associated with consumption of raw oysters. In the summer of 2015, Canada experienced the largest outbreak associated with the consumption of raw oysters harvested from British Columbia (BC) coastal waters.

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Background: People with diabetes mellitus (DM) have increased infection risk. The healthcare utilization of pediatric and adolescent diabetic patients with infection is not well defined. This study evaluates the number of pediatric and adolescent patients with DM that seek medical treatment for infection management and assesses its socioeconomic impact.

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During July-October 2014, an outbreak of 119 Escherichia coli O157:H7 infections in Alberta, Canada was identified through notifiable disease surveillance and investigated by local, provincial, and federal public health and food regulatory agencies. Twenty-three (19%) patients were hospitalized, six of whom developed hemolytic uremic syndrome; no deaths were reported. Informed by case interviews, seven potential food sources were identified and investigated.

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What Is Already Known About This Topic?: Pork is a known, although infrequent, source of human O157:H7 infection. O157:H7 infections often result in clinically severe illness with serious complications in humans.

What Is Added By This Report?: During July-October 2014, an outbreak of 119 cases of O157:H7 infections associated with exposure to contaminated pork products occurred in Alberta, Canada.

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The mechanics of hMSH2-hMSH6 ATP binding and hydrolysis are critical to several proposed mechanisms for mismatch repair (MMR), which in turn rely on the detailed coordination of ATP processing between the individual hMSH2 and hMSH6 subunits. Here we show that hMSH2-hMSH6 is strictly controlled by hMSH2 and magnesium in a complex with ADP (hMSH2(magnesium-ADP)-hMSH6). Destabilization of magnesium results in ADP release from hMSH2 that allows high affinity ATP binding by hMSH6, which then enhances ATP binding by hMSH2.

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