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United States Department of Agriculture

Agricultural Research Service

Research Project: NOVEL DISEASE CONTROL STRATEGIES FOR CELLULAR AND SUB-CELLULAR PATHOGENS

Location: Molecular Plant Pathology

Title: Analysis of the solvent accessibility of cysteine residues on maize rayado fino virus virus-like particles produced in Nicotiana benthamiana plants and cross-linking of peptides to VLPs

Authors
item Natilla, Angela
item Hammond, Rosemarie

Submitted to: Journal of Visualized Experiments
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: July 13, 2012
Publication Date: February 13, 2013
Citation: Natilla, A., Hammond, R. 2013. Analysis of the solvent accessibility of cysteine residues on maize rayado fino virus virus-like particles produced in Nicotiana benthamiana plants and cross-linking of peptides to VLPs. Journal of Visualized Experiments. 72:e50084.

Interpretive Summary: Agricultural losses due to plant and animal diseases necessitate the development of reagents for detection and control of the pathogens that cause the disease. Plant viruses and virus-like particles are able to assemble themselves in unique ways. Mimicking and exploiting virus biological, chemical, and physical properties holds promise to provide solutions to some of the world’s most pressing challenges in agriculture and medicine; however, in order to utilize viruses for the new applications, they must be modified from their natural form to impart the new functions. In this report, we describe the steps to determine which properties of the virus can be modified and the methods used to chemically modify the viruses to serve as platforms for attachment and display of novel reagents. These results will be of interest to plant and animal virologists who are studying virus particle assembly and nanotechnology, and disease specialists who are developing methods for disease control.

Technical Abstract: A method to analyze the solvent accessibility of the thiol group of cysteine residues of Maize rayado fino virus-virus-like particles (VLPs) followed by a peptide cross-linking reaction is described. The method takes advantage of the availability of several chemical groups on the surface of the VLPs which can be a target for specific reactions.

Last Modified: 9/20/2014
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