Pathogen receptor discovery with a microfluidic human membrane protein array

The discovery of how a pathogen invades a cell requires one to determine which host cell receptors are exploited. This determination is a challenging problem because the receptor is invariably a membrane protein, which represents an Achilles heel in proteomics. We have developed a universal platform...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2016-04, Vol.113 (16), p.4344-4349
Main Authors: Glick, Yair, Ben-Ari, Ya’ara, Drayman, Nir, Pellach, Michal, Neveu, Gregory, Boonyaratanakornkit, Jim, Avrahami, Dorit, Einav, Shirit, Oppenheim, Ariella, Gerber, Doron
Format: Article
Language:English
Subjects:
Arrays
Biological Sciences
Humans
Membranes
Microfluidic Analytical Techniques - methods
Pathogens
Protein Array Analysis - methods
Proteins
Proteomics
Proteomics - methods
Receptors, Virus - metabolism
Simian virus 40 - metabolism
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Summary:The discovery of how a pathogen invades a cell requires one to determine which host cell receptors are exploited. This determination is a challenging problem because the receptor is invariably a membrane protein, which represents an Achilles heel in proteomics. We have developed a universal platform for high-throughput expression and interaction studies of membrane proteins by creating a microfluidic-based comprehensive human membrane protein array (MPA). The MPA is, to our knowledge, the first of its kind and offers a powerful alternative to conventional proteomics by enabling the simultaneous study of 2,100 membrane proteins. We characterized direct interactions of a whole nonenveloped virus (simian virus 40), as well as those of the hepatitis delta enveloped virus large form antigen, with candidate host receptors expressed on the MPA. Selected newly discovered membrane protein–pathogen interactions were validated by conventional methods, demonstrating that the MPA is an important tool for cellular receptor discovery and for understanding pathogen tropism.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1518698113