학술논문

Purification and characterization of HIV–human protein complexes
Document Type
Article
Source
Methods. Jan2011, Vol. 53 Issue 1, p13-19. 7p.
Subject
*HIV
*COMPLEX compounds
*PATHOGENIC microorganisms
*GENE mapping
*PROTEIN-protein interactions
*MASS spectrometry
*VIRAL replication
*PROTEOMICS
Language
ISSN
1046-2023
Abstract
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. [ABSTRACT FROM AUTHOR]