Available Technology
Determination of intracellular protein-protein interactions
Technology:
Novel method for assaying protein-protein, protein-nucleic acid, protein-membrane and protein-carbohydrate interaction
Markets Addressed
This novel method can be used to screen a variety of libraries to identify associations relevant to human diseases, including proliferative diseases (e.g. cancer):
• Assay protein-protein, protein-nucleic acid, protein-membrane and protein-carbohydrate associations
• Identify agents that modulate (e.g., increase or decrease) these associations
• Detect interactions involving secondary modifications
• Identify agents that modulate aberrant cellular proliferation
Innovations and Advantages
Dr. Nibert developed a novel method for assaying protein-protein, protein-nucleic acid, protein-membrane and protein-carbohydrate interactions. The method takes advantage of replication machinery of the reovirus, which replicate in distinctive, cytoplasmic inclusion bodies. Recent evidence from the Nibert laboratory has shown that a single reovirus protein, microNS, is sufficient for forming inclusion bodies in the cytoplasm of transfected cells. MicroNS is known to associate with and recruit viral proteins to these inclusion bodies. Colocalization in inclusion bodies is currently being used to identify associations between viral proteins.
In the present invention, the technology platform is extended to detect associations between any two proteins, as well as protein-nucleic acid, protein-membrane and protein-carbohydrate interactions. Researchers in Dr. Nibert’s laboratory fused a protein of interest as well as green fluorescent protein (GFP; reporter gene) to the µNS protein. Proteins, nucleic acids and carbohydrates that bind to the fused protein will be recruited and localized to inclusion bodies, and concluded to associate with the fused protein.
This screening method has advantages over existing technologies:
• Detect interactions using fluorescent microscopy. Use of fluorescence has the potential for multiple color read-outs and is simpler than using non-fluorescent reporter assays for the yeast-2-hybrid screen.
• Detect interactions involving secondary modifications (e.g. phosphorylation, acetylation, proteolysis) that may not be detectable in yeast-based systems.
• Screen does not rely on nuclear translocation and transcriptional activations and therefore offers improved sensitivity to cytoplasmic interactions.
Additional Information
Intellectual Property Status: Patent(s) pending
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Inventor(s):
Arnold, Michelle M.
Broering, Teresa J.
Miller, Cathy Lea
Nibert, Max L.
Categories:
For further information, please contact:
Michal Preminger, Director of Business Development
(617) 432-0920
Reference Harvard Case #2384