Nash, Tara , Lopez-Ochoa, Luisa , Hanley-Bowdoin, Linda .
Peptide aptamers that bind to the protein interaction domain of a geminivirus replication protein.
Geminiviruses are a large family of single-stranded DNA viruses that cause losses of food and cash crops around the world. They can recombine with other geminiviruses and frequently occur as mixed infections. As a consequence, an effective resistance strategy must be able to target multiple and rapidly evolving geminiviruses. We are investigating the efficacy of using peptide aptamers that bind and interfere with the highly conserved geminivirus replication protein (Rep) to confer broad-based resistance. The central region of Rep is of specific interest because of the variety of protein interactions that have been mapped to this region. Rep forms oligomers with itself and binds to the viral replication enhancer protein AL3 and to a number of host proteins, including PCNA, pRBR, Grik, Grimp, and UBC9. A yeast two-hybrid screen of a library containing 20-mer random peptide sequences in the active site of bacterial thioredoxin (Trx) identified 500 aptamers that bind to the full length Rep protein of Tomato Golden Mosaic Virus. The binding sites of 222 aptamers were mapped using a series of baits corresponding to different domains of Rep. Of the aptamers tested, 173 were confirmed for Rep binding, 101 of which interacted with specific Rep domains while 72 recognized multiple domains. Ninety-four aptamers bound the Rep protein interaction domain. The sequenced peptide are currently being analyzed for shared motifs and homology to known Rep partners and plant host proteins.
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1 - North Carolina State University, Molecular and Structural Biochemistry, Viral Genomics, Campus Box 7651, Raleigh, NC, 27695, USA
2 - North Carolina State University, Molecular and Structural Biochemistry
Presentation Type: Plant Biology Abstract
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM