Authors
Stefanie Jaeger, Peter Cimermancic, Natali Gulbahce, Jeffrey R Johnson, Kathryn E McGovern, Starlynn C Clarke, Michael Shales, Gaelle Mercenne, Lars Pache, Kathy Li, Hilda Hernandez, Gwendolyn M Jang, Shoshannah L Roth, Eyal Akiva, John Marlett, Melanie Stephens, Iván D’Orso, Jason Fernandes, Marie Fahey, Cathal Mahon, Anthony J O’Donoghue, Aleksandar Todorovic, John H Morris, David A Maltby, Tom Alber, Gerard Cagney, Frederic D Bushman, John A Young, Sumit K Chanda, Wesley I Sundquist, Tanja Kortemme, Ryan D Hernandez, Charles S Craik, Alma Burlingame, Andrej Sali, Alan D Frankel, Nevan J Krogan
Publication date
2012/1/19
Journal
Nature
Volume
481
Issue
7381
Pages
365-370
Publisher
Nature Publishing Group UK
Description
Human immunodeficiency virus (HIV) has a small genome and therefore relies heavily on the host cellular machinery to replicate. Identifying which host proteins and complexes come into physical contact with the viral proteins is crucial for a comprehensive understanding of how HIV rewires the host’s cellular machinery during the course of infection. Here we report the use of affinity tagging and purification mass spectrometry,, to determine systematically the physical interactions of all 18 HIV-1 proteins and polyproteins with host proteins in two different human cell lines (HEK293 and Jurkat). Using a quantitative scoring system that we call MiST, we identified with high confidence 497 HIV–human protein–protein interactions involving 435 individual human proteins, with ∼40% of the interactions being identified in both cell types. We found that the host proteins hijacked by HIV, especially those found interacting in …
Total citations
Scholar articles
S Jaeger, P Cimermancic, N Gulbahce, JR Johnson… - Nature, 2012