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A catalogue of putative HIV-1 protease host cell substrates

Francis Impens UGent, Evy Timmerman UGent, An Staes UGent, Kathleen Moens UGent, Kevin Ariën UGent, Bruno Verhasselt UGent, Joël Vandekerckhove UGent and Kris Gevaert UGent (2012) BIOLOGICAL CHEMISTRY. 393(9). p.915-931
abstract
Processing of human immunodeficiency virus (HIV) proteins by the HIV-1 protease is essential for HIV infectivity. In addition, several studies have revealed cleavage of human proteins by this viral protease during infection; however, no large-scale HIV-1 protease degradomics study has yet been performed. To identify putative host substrates in an unbiased manner and on a proteome-wide scale, we used positional proteomics to identify peptides reporting protein processing by the HIV-1 protease, and a catalogue of over 120 cellular HIV-1 protease substrates processed in vitro was generated. This catalogue includes previously reported substrates as well as recently described interaction partners of HIV-1 proteins. Cleavage site alignments revealed a specificity profile in good correlation with previous studies, even though the ELLE consensus motif was not cleaved efficiently when incorporated into peptide substrates due to subsite cooperativity. Our results are further discussed in the context of HIV-1 infection and the complex substrate recognition by the viral protease.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
AIDS, COFRADIC, positional proteomics, protease degradomics, protein neo-N-termini, subsite cooperativity, N-TERMINAL PEPTIDES, HUMAN-IMMUNODEFICIENCY-VIRUS, SPECIFICITY, TYPE-1, IDENTIFICATION, PROTEOMICS, CLEAVAGE, IN-VIVO, AMINO-ACIDS, FRACTIONAL DIAGONAL CHROMATOGRAPHY
journal title
BIOLOGICAL CHEMISTRY
Biol. Chem.
volume
393
issue
9
pages
915 - 931
Web of Science type
Article
Web of Science id
000307509500008
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
2.683 (2012)
JCR rank
158/288 (2012)
JCR quartile
3 (2012)
ISSN
1431-6730
DOI
10.1515/hsz-2012-0168
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
3034664
handle
http://hdl.handle.net/1854/LU-3034664
date created
2012-10-25 15:49:30
date last changed
2012-11-05 11:53:03
@article{3034664,
  abstract     = {Processing of human immunodeficiency virus (HIV) proteins by the HIV-1 protease is essential for HIV infectivity. In addition, several studies have revealed cleavage of human proteins by this viral protease during infection; however, no large-scale HIV-1 protease degradomics study has yet been performed. To identify putative host substrates in an unbiased manner and on a proteome-wide scale, we used positional proteomics to identify peptides reporting protein processing by the HIV-1 protease, and a catalogue of over 120 cellular HIV-1 protease substrates processed in vitro was generated. This catalogue includes previously reported substrates as well as recently described interaction partners of HIV-1 proteins. Cleavage site alignments revealed a specificity profile in good correlation with previous studies, even though the ELLE consensus motif was not cleaved efficiently when incorporated into peptide substrates due to subsite cooperativity. Our results are further discussed in the context of HIV-1 infection and the complex substrate recognition by the viral protease.},
  author       = {Impens, Francis and Timmerman, Evy and Staes, An and Moens, Kathleen and Ari{\"e}n, Kevin and Verhasselt, Bruno and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1431-6730},
  journal      = {BIOLOGICAL CHEMISTRY},
  keyword      = {AIDS,COFRADIC,positional proteomics,protease degradomics,protein neo-N-termini,subsite cooperativity,N-TERMINAL PEPTIDES,HUMAN-IMMUNODEFICIENCY-VIRUS,SPECIFICITY,TYPE-1,IDENTIFICATION,PROTEOMICS,CLEAVAGE,IN-VIVO,AMINO-ACIDS,FRACTIONAL DIAGONAL CHROMATOGRAPHY},
  language     = {eng},
  number       = {9},
  pages        = {915--931},
  title        = {A catalogue of putative HIV-1 protease host cell substrates},
  url          = {http://dx.doi.org/10.1515/hsz-2012-0168},
  volume       = {393},
  year         = {2012},
}

Chicago
Impens, Francis, Evy Timmerman, An Staes, Kathleen Moens, Kevin Ariën, Bruno Verhasselt, Joël Vandekerckhove, and Kris Gevaert. 2012. “A Catalogue of Putative HIV-1 Protease Host Cell Substrates.” Biological Chemistry 393 (9): 915–931.
APA
Impens, F., Timmerman, E., Staes, A., Moens, K., Ariën, K., Verhasselt, B., Vandekerckhove, J., et al. (2012). A catalogue of putative HIV-1 protease host cell substrates. BIOLOGICAL CHEMISTRY, 393(9), 915–931.
Vancouver
1.
Impens F, Timmerman E, Staes A, Moens K, Ariën K, Verhasselt B, et al. A catalogue of putative HIV-1 protease host cell substrates. BIOLOGICAL CHEMISTRY. 2012;393(9):915–31.
MLA
Impens, Francis, Evy Timmerman, An Staes, et al. “A Catalogue of Putative HIV-1 Protease Host Cell Substrates.” BIOLOGICAL CHEMISTRY 393.9 (2012): 915–931. Print.