Hauptseite > Publikationsdatenbank > Human immunodeficiency virus type 1 Vpr: Oligomerization is an essential feature for its incorporation into virus particles > print

001     13094
005     20200402205938.0
024 7 _ |2 pmid
|a pmid:20529298
024 7 _ |2 pmc
|a pmc:PMC2894018
024 7 _ |2 DOI
|a 10.1186/1743-422X-7-119
024 7 _ |2 WOS
|a WOS:000244272500011
037 _ _ |a PreJuSER-13094
041 _ _ |a eng
082 _ _ |a 610
084 _ _ |2 WoS
|a Virology
100 1 _ |a Venkatachari, N.J.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Human immunodeficiency virus type 1 Vpr: Oligomerization is an essential feature for its incorporation into virus particles
260 _ _ |a San Diego, Calif. [u.a.]
|b Elsevier
|c 2010
300 _ _ |a 119
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Virology
|x 0042-6822
|0 23403
|v 7
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a HIV-1 Vpr, a nonstructural viral protein associated with virus particles, has a positive role in the efficient transport of PIC into the nucleus of non-dividing target cells and enhances virus replication in primary T cells. Vpr is a 96 amino acid protein and the structure by NMR shows three helical domains. Vpr has been shown to exist as dimers and higher order oligomers. Considering the multifunctional nature of Vpr, the contribution of distinct helical domains to the dimer/oligomer structure of Vpr and the relevance of this feature to its functions are not clear. To address this, we have utilized molecular modeling approaches to identify putative models of oligomerization. The predicted interface residues were subjected to site-directed mutagenesis and evaluated their role in intermolecular interaction and virion incorporation. The interaction between Vpr molecules was monitored by Bimolecular Fluorescence complementation (BiFC) method. The results show that Vpr forms oligomers in live cells and residues in helical domains play critical roles in oligomerization. Interestingly, Vpr molecules defective in oligomerization also fail to incorporate into the virus particles. Based on the data, we suggest that oligomerization of Vpr is essential for virion incorporation property and may also have a role in the events associated with virus infection.
536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK505
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Cell Line
650 _ 2 |2 MeSH
|a HIV-1: chemistry
650 _ 2 |2 MeSH
|a HIV-1: genetics
650 _ 2 |2 MeSH
|a HIV-1: metabolism
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Molecular Conformation
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Sequence Alignment
650 _ 2 |2 MeSH
|a Virion: chemistry
650 _ 2 |2 MeSH
|a Virion: genetics
650 _ 2 |2 MeSH
|a Virion: metabolism
650 _ 2 |2 MeSH
|a vpr Gene Products, Human Immunodeficiency Virus: chemistry
650 _ 2 |2 MeSH
|a vpr Gene Products, Human Immunodeficiency Virus: genetics
650 _ 2 |2 MeSH
|a vpr Gene Products, Human Immunodeficiency Virus: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a vpr Gene Products, Human Immunodeficiency Virus
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a HIV-1 Vpr
653 2 0 |2 Author
|a CD28
653 2 0 |2 Author
|a CTLA-4
653 2 0 |2 Author
|a IFN-gamma
653 2 0 |2 Author
|a NF-kappa B
653 2 0 |2 Author
|a immune activation
700 1 _ |a Walker, L.A.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Tastan, O.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Le, T.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Dempsey, T.M.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Li, Y.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Yanamala, N.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Srinivasan, A.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Klein-Seetharaman, J.
|b 8
|u FZJ
|0 P:(DE-Juel1)VDB44599
700 1 _ |a Montelaro, R.C.
|b 9
|0 P:(DE-HGF)0
700 1 _ |a Ayyavoo, V.
|b 10
|0 P:(DE-HGF)0
773 _ _ |a 10.1186/1743-422X-7-119
|g Vol. 7, p. 119
|p 119
|q 7<119
|0 PERI:(DE-600)1471925-3
|t Virology
|v 7
|y 2010
|x 0042-6822
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2894018
909 C O |o oai:juser.fz-juelich.de:13094
|p VDB
913 1 _ |k P45
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|l Biologische Informationsverarbeitung
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK505
|x 0
913 2 _ |a DE-HGF
|b Key Technologies
|l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences
|1 G:(DE-HGF)POF3-550
|0 G:(DE-HGF)POF3-551
|2 G:(DE-HGF)POF3-500
|v Functional Macromolecules and Complexes
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k ISB-2
|l Molekulare Biophysik
|d 31.12.2010
|g ISB
|0 I:(DE-Juel1)ISB-2-20090406
|x 0
970 _ _ |a VDB:(DE-Juel1)124921
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)ISB-2-20090406

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