Date of Award

5-2015

Degree Type

Thesis

Degree Name

Departmental Honors

Department

Biology

First Advisor

Bart Tarbet

Abstract

Millions of people die each year from infectious diseases. This is partly due to the difficulty of transporting temperature dependent vaccines through what is called the cold chain in developing countries. I hypothesize that we can increase vaccine accessibility by finding cost effective alternatives to vaccine production and by eliminating the cold chain through vaccine stabilizers. The gold standard in purification of influenza virus is by means of ultracentrifugation. Although effective, this process is very expensive and thus impractical for developing countries. I hypothesize that column chromatography can be a cost efficient alternative that is as effective as ultracentrifugation. The purification ability of column chromatography was tested by comparing two different chromatography resins. The Capto Q resin separates proteins on the basis of protein charge. The Capto 700 resin separates proteins on the basis of both size and charge. It was found that while protein separation occurred, more research will be required to assure full viral protein purification.

It is hypothesized that vaccine stabilizers can be used to eliminate the cold chain. The effect of the gelatin on inactivated influenza virus vaccines was evaluated using hemagglutinin (HA) assays and neuraminidase (NA) assays. The assays evaluate viral protein activity in samples exposed to elevated temperatures for set periods of time (1 min, 5 min, 10 min, 20 min, 40 min, 60 min, 120 min, 240 min, 300 min, and 360 min). Elevated temperatures (45, 52, and 60 degrees Celsius) facilitated an accelerated stability test, which simulates extended effects of time on vaccines. In addition to testing different temperatures, the following concentrations of collagen were used as percent by total volume: 0.3%, 1%, 3%, and 10%. These were tested for optimizing the stabilization of the vaccine. The results of the neuraminidase assay show that 3% collagen significantly increased the stability of the vaccine by approximately 10,000 fold.

Included in

Biology Commons

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