Purification and characterization of HIV-human protein complexes

Stefanie Jäger, Natali Gulbahce, Peter Cimermancic, Joshua Kane, Nanhai He, Seemay Chou, Iván D'Orso, Jason Fernandes, Gwendolyn Jang, Alan D. Frankel, Tom Alber, Qiang Zhou, Nevan J. Krogan

Research output: Contribution to journalArticle

41 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)13-19
Number of pages7
JournalMethods
Volume53
Issue number1
DOIs
StatePublished - Jan 2011

Fingerprint

Human Immunodeficiency Virus Proteins
Purification
Proteins
Viral Proteins
Pathogens
Mass Spectrometry
Protein Interaction Maps
Biological Phenomena
Viral Genome
Mass spectrometry
Genes
Yeasts
HIV
Genome
Databases
Viruses
Yeast

Keywords

  • HIV
  • Mass spectrometry
  • Protein interaction
  • Proteomics
  • Virus-host interaction

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Jäger, S., Gulbahce, N., Cimermancic, P., Kane, J., He, N., Chou, S., ... Krogan, N. J. (2011). Purification and characterization of HIV-human protein complexes. Methods, 53(1), 13-19. https://doi.org/10.1016/j.ymeth.2010.08.007

Purification and characterization of HIV-human protein complexes. / Jäger, Stefanie; Gulbahce, Natali; Cimermancic, Peter; Kane, Joshua; He, Nanhai; Chou, Seemay; D'Orso, Iván; Fernandes, Jason; Jang, Gwendolyn; Frankel, Alan D.; Alber, Tom; Zhou, Qiang; Krogan, Nevan J.

In: Methods, Vol. 53, No. 1, 01.2011, p. 13-19.

Research output: Contribution to journalArticle

Jäger, S, Gulbahce, N, Cimermancic, P, Kane, J, He, N, Chou, S, D'Orso, I, Fernandes, J, Jang, G, Frankel, AD, Alber, T, Zhou, Q & Krogan, NJ 2011, 'Purification and characterization of HIV-human protein complexes', Methods, vol. 53, no. 1, pp. 13-19. https://doi.org/10.1016/j.ymeth.2010.08.007
Jäger S, Gulbahce N, Cimermancic P, Kane J, He N, Chou S et al. Purification and characterization of HIV-human protein complexes. Methods. 2011 Jan;53(1):13-19. https://doi.org/10.1016/j.ymeth.2010.08.007
Jäger, Stefanie ; Gulbahce, Natali ; Cimermancic, Peter ; Kane, Joshua ; He, Nanhai ; Chou, Seemay ; D'Orso, Iván ; Fernandes, Jason ; Jang, Gwendolyn ; Frankel, Alan D. ; Alber, Tom ; Zhou, Qiang ; Krogan, Nevan J. / Purification and characterization of HIV-human protein complexes. In: Methods. 2011 ; Vol. 53, No. 1. pp. 13-19.
@article{66f2d1c98e2d4c47bdeea1d9b49dd26c,
title = "Purification and characterization of HIV-human protein complexes",
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.",
keywords = "HIV, Mass spectrometry, Protein interaction, Proteomics, Virus-host interaction",
author = "Stefanie J{\"a}ger and Natali Gulbahce and Peter Cimermancic and Joshua Kane and Nanhai He and Seemay Chou and Iv{\'a}n D'Orso and Jason Fernandes and Gwendolyn Jang and Frankel, {Alan D.} and Tom Alber and Qiang Zhou and Krogan, {Nevan J.}",
year = "2011",
month = "1",
doi = "10.1016/j.ymeth.2010.08.007",
language = "English (US)",
volume = "53",
pages = "13--19",
journal = "Methods in Enzymology",
issn = "0076-6879",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Purification and characterization of HIV-human protein complexes

AU - Jäger, Stefanie

AU - Gulbahce, Natali

AU - Cimermancic, Peter

AU - Kane, Joshua

AU - He, Nanhai

AU - Chou, Seemay

AU - D'Orso, Iván

AU - Fernandes, Jason

AU - Jang, Gwendolyn

AU - Frankel, Alan D.

AU - Alber, Tom

AU - Zhou, Qiang

AU - Krogan, Nevan J.

PY - 2011/1

Y1 - 2011/1

N2 - 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.

AB - 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.

KW - HIV

KW - Mass spectrometry

KW - Protein interaction

KW - Proteomics

KW - Virus-host interaction

UR - http://www.scopus.com/inward/record.url?scp=78651501511&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78651501511&partnerID=8YFLogxK

U2 - 10.1016/j.ymeth.2010.08.007

DO - 10.1016/j.ymeth.2010.08.007

M3 - Article

C2 - 20708689

AN - SCOPUS:78651501511

VL - 53

SP - 13

EP - 19

JO - Methods in Enzymology

JF - Methods in Enzymology

SN - 0076-6879

IS - 1

ER -