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Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis

Delphine Lavens UGent, Frank Peelman UGent, José Van Der Heyden UGent, Isabel Uyttendaele UGent, Dominiek Catteeuw UGent, Annick Verhee UGent, B Van Schoubroeck, J Kurth, S Hallenberger and R Clayton, et al. (2010) NUCLEIC ACIDS RESEARCH. 38(6). p.1902-1912
abstract
The host restriction factor Apobec3G is a cytidine deaminase that incorporates into HIV-1 virions and interferes with viral replication. The HIV-1 accessory protein Vif subverts Apobec3G by targeting it for proteasomal degradation. We propose a model in which Apobec3G N-terminal domains symmetrically interact via a head-to-head interface containing residues 122 RLYYFW 127. To validate this model and to characterize the Apobec3G-Apobec3G and the Apobec3G-Vif interactions, the mammalian protein-protein interaction trap two-hybrid technique was used. Mutations in the head-to-head interface abrogate the Apobec3G-Apobec3G interaction. All mutations that inhibit Apobec3G-Apobec3G binding also inhibit the Apobec3G-Vif interaction, indicating that the head-to head interface plays an important role in the interaction with Vif. Only the D128K, P129A and T32Q mutations specifically affect the Apobec3G-Vif association. In our model, D128, P129 and T32 cluster at the edge of the head-to-head interface, possibly forming a Vif binding site composed of two Apobec3G molecules. We propose that Vif either binds at the Apobec3G head-to-head interface or associates with an RNA-stabilized Apobec3G oligomer.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
LEPTIN RECEPTOR, INTERACTION TRAP, ANTIVIRAL ACTIVITY, VIRION INFECTIVITY FACTOR, FUNCTIONAL IMPLICATIONS, CRYSTAL-STRUCTURE, PROTEIN, VIRUS TYPE-1 VIF, CATALYTIC DOMAIN, MAMMALIAN-CELLS
journal title
NUCLEIC ACIDS RESEARCH
Nucleic Acids Res.
volume
38
issue
6
pages
11 pages
Web of Science type
Article
Web of Science id
000276304600022
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
7.836 (2010)
JCR rank
30/284 (2010)
JCR quartile
1 (2010)
ISSN
0305-1048
DOI
10.1093/nar/gkp1154
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
943512
handle
http://hdl.handle.net/1854/LU-943512
date created
2010-05-06 11:28:10
date last changed
2013-01-30 09:41:28
@article{943512,
  abstract     = {The host restriction factor Apobec3G is a cytidine deaminase that incorporates into HIV-1 virions and interferes with viral replication. The HIV-1 accessory protein Vif subverts Apobec3G by targeting it for proteasomal degradation. We propose a model in which Apobec3G N-terminal domains symmetrically interact via a head-to-head interface containing residues 122 RLYYFW 127. To validate this model and to characterize the Apobec3G-Apobec3G and the Apobec3G-Vif interactions, the mammalian protein-protein interaction trap two-hybrid technique was used. Mutations in the head-to-head interface abrogate the Apobec3G-Apobec3G interaction. All mutations that inhibit Apobec3G-Apobec3G binding also inhibit the Apobec3G-Vif interaction, indicating that the head-to head interface plays an important role in the interaction with Vif. Only the D128K, P129A and T32Q mutations specifically affect the Apobec3G-Vif association. In our model, D128, P129 and T32 cluster at the edge of the head-to-head interface, possibly forming a Vif binding site composed of two Apobec3G molecules. We propose that Vif either binds at the Apobec3G head-to-head interface or associates with an RNA-stabilized Apobec3G oligomer.},
  author       = {Lavens, Delphine and Peelman, Frank and Van Der Heyden, Jos{\'e} and Uyttendaele, Isabel and Catteeuw, Dominiek and Verhee, Annick and Van Schoubroeck, B and Kurth, J and Hallenberger, S and Clayton, R and Tavernier, Jan},
  issn         = {0305-1048},
  journal      = {NUCLEIC ACIDS RESEARCH},
  keyword      = {LEPTIN RECEPTOR,INTERACTION TRAP,ANTIVIRAL ACTIVITY,VIRION INFECTIVITY FACTOR,FUNCTIONAL IMPLICATIONS,CRYSTAL-STRUCTURE,PROTEIN,VIRUS TYPE-1 VIF,CATALYTIC DOMAIN,MAMMALIAN-CELLS},
  language     = {eng},
  number       = {6},
  pages        = {1902--1912},
  title        = {Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis},
  url          = {http://dx.doi.org/10.1093/nar/gkp1154},
  volume       = {38},
  year         = {2010},
}

Chicago
Lavens, Delphine, Frank Peelman, José Van Der Heyden, Isabel Uyttendaele, Dominiek Catteeuw, Annick Verhee, B Van Schoubroeck, et al. 2010. “Definition of the Interacting Interfaces of Apobec3G and HIV-1 Vif Using MAPPIT Mutagenesis Analysis.” Nucleic Acids Research 38 (6): 1902–1912.
APA
Lavens, D., Peelman, F., Van Der Heyden, J., Uyttendaele, I., Catteeuw, D., Verhee, A., Van Schoubroeck, B., et al. (2010). Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis. NUCLEIC ACIDS RESEARCH, 38(6), 1902–1912.
Vancouver
1.
Lavens D, Peelman F, Van Der Heyden J, Uyttendaele I, Catteeuw D, Verhee A, et al. Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis. NUCLEIC ACIDS RESEARCH. 2010;38(6):1902–12.
MLA
Lavens, Delphine, Frank Peelman, José Van Der Heyden, et al. “Definition of the Interacting Interfaces of Apobec3G and HIV-1 Vif Using MAPPIT Mutagenesis Analysis.” NUCLEIC ACIDS RESEARCH 38.6 (2010): 1902–1912. Print.