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Methods. 2011 Jan;53(1):13-9. doi: 10.1016/j.ymeth.2010.08.007. Epub 2010 Aug 12.

Purification and characterization of HIV-human protein complexes.

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  • 1Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 1700 4th Street, San Francisco, CA 94158, USA.

Abstract

To fully understand how pathogens infect their host and hijack key biological processes, systematic mapping of intra-pathogenic and pathogen-host protein-protein interactions (PPIs) is crucial. Due to the relatively small size of viral genomes (usually around 10-100 proteins), generation of comprehensive host-virus PPI maps using different experimental platforms, including affinity tag purification-mass spectrometry (AP-MS) and yeast two-hybrid (Y2H) approaches, can be achieved. Global maps such as these provide unbiased insight into the molecular mechanisms of viral entry, replication and assembly. However, to date, only two-hybrid methodology has been used in a systematic fashion to characterize viral-host protein-protein interactions, although a deluge of data exists in databases that manually curate from the literature individual host-pathogen PPIs. We will summarize this work and also describe an AP-MS platform that can be used to characterize viral-human protein complexes and discuss its application for the HIV genome.

Copyright © 2010. Published by Elsevier Inc.

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