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Virology. 2014 Jul;460-461:194-206. doi: 10.1016/j.virol.2014.04.038. Epub 2014 Jun 10.

Proteome analysis of the HIV-1 Gag interactome.

Author information

1
Department of Infectious Diseases, Virology, Universitätsklinikum Heidelberg, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany. Electronic address: christine.engeland@urz.uni-heidelberg.de.
2
Bioquant, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany. Electronic address: nigel.brown@bioquant.uni-heidelberg.de.
3
Department of Infectious Diseases, Virology, Universitätsklinikum Heidelberg, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany; Bioquant, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany. Electronic address: kathleen.boerner@med.uni-heidelberg.de.
4
Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, D-13125 Berlin, Germany. Electronic address: schuemann@fmp-berlin.de.
5
Leibniz-Institut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, D-13125 Berlin, Germany. Electronic address: ekrause@fmp-berlin.de.
6
Institute for Medical Informatics and Biometry (IMB), Medical Faculty Carl Gustav Carus, Dresden University of Technology, Fetscherstraße 74, D-01307 Dresden, Germany. Electronic address: lars.kaderali@tu-dresden.de.
7
Molecular Oncology, Medical School, University of Leipzig, Semmelweisstraße 14, D-04103 Leipzig, Germany. Electronic address: Gerd.Mueller@medizin.uni-leipzig.de.
8
Department of Infectious Diseases, Virology, Universitätsklinikum Heidelberg, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany. Electronic address: Hans-Georg.Kraeusslich@med.uni-heidelberg.de.

Abstract

Human immunodeficiency virus Gag drives assembly of virions in infected cells and interacts with host factors which facilitate or restrict viral replication. Although several Gag-binding proteins have been characterized, understanding of virus-host interactions remains incomplete. In a series of six affinity purification screens, we have identified protein candidates for interaction with HIV-1 Gag. Proteins previously found in virions or identified in siRNA screens for host factors influencing HIV-1 replication were recovered. Helicases, translation factors, cytoskeletal and motor proteins, factors involved in RNA degradation and RNA interference were enriched in the interaction data. Cellular networks of cytoskeleton, SR proteins and tRNA synthetases were identified. Most prominently, components of cytoplasmic RNA transport granules were co-purified with Gag. This study provides a survey of known Gag-host interactions and identifies novel Gag binding candidates. These factors are associated with distinct molecular functions and cellular pathways relevant in host-pathogen interactions.

KEYWORDS:

HIV Gag; Virus–host interactions

PMID:
25010285
DOI:
10.1016/j.virol.2014.04.038
[Indexed for MEDLINE]
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