Norovirus causes almost 90% of epidemic, non-bacterial
outbreaks of gastroenteritis around the world. Extremely infectious and diverse,
the virus causes acute diarrhea, vomiting, abdominal cramps, headache, fatigue,
and fever. Though the illness is generally resolved within 48 hours, mortalities
do occur in the young, elderly, and immune-compromised, as a result of
complications brought on by dehydration.
In spite of the high prevalence of norovirus infections,
there is still no vaccine available to prevent the disease. Progress is hindered
by a lack of a suitable animal model and low reproduction rates in cell culture.
However, the capsid protein of norovirus has been successfully expressed in
plant and insect cells; these proteins present an alternative method for vaccine
production. To make this option viable, a cost effective purification scheme for
these proteins must be realized.
Researchers at the Biodesign Institute at Arizona State
University have developed a peptide ligand selection technique to isolate
protein components of norovirus for vaccine development. This technique utilizes
a library of 10,000 peptides which are 20 amino acids long-a sufficient library
size due to the presence of all possible dimers, trimers, and 60% of all
possible tetramers. The increased affinity of the longer peptides also enables
low sample consumption and generation of fewer false positives. High affinity
binding peptides can then be used for vaccine development as purification tools
for recombinant proteins.
Potential Applications
- Vaccine development
- Purification
- New detection materials
Benefits and Advantages
- Convenient: No need for bulky labeling groups
- Fast: Highly diverse library allows quick identification
of high affinity peptides
- Accurate: Low rate of false positives
- Low sample consumption: Micrograms of sample
needed
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For more information about the inventor(s) and their
research, please see
Dr.
Diehnelt's directory webpage
Dr.
Johnston's directory webpage
