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Titolo:
Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor
Autore:
Evans, DT; Tillman, KC; Desrosiers, RC;
Indirizzi:
Harvard Univ, New England Reg Primate Res Ctr, Sch Med, Southborough, MA 01772 USA Harvard Univ Southborough MA USA 01772 ch Med, Southborough, MA 01772 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 1, volume: 76, anno: 2002,
pagine: 327 - 337
SICI:
0022-538X(200201)76:1<327:EGCDFD>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIMIAN IMMUNODEFICIENCY VIRUS; PATHOGENIC MOLECULAR CLONE; TRANSMEMBRANE PROTEIN; INTERNALIZATION SIGNAL; TYPE-1 MATRIX; CELL-SURFACE; HIV-1 GP41; EXPRESSION; TAIL; CALMODULIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Desrosiers, RC Harvard Univ, New England Reg Primate Res Ctr, Sch Med, 1 Pine Hill Dr, Southborough, MA 01772 USA Harvard Univ 1 Pine Hill Dr Southborough MA USA 01772 2 USA
Citazione:
D.T. Evans et al., "Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor", J VIROLOGY, 76(1), 2002, pp. 327-337

Abstract

Lentivirus envelope glycoproteins have unusually long cytoplasmic domains compared to those of other retroviruses. To identify cellular binding partners of the simian immunodeficiency virus (SIV) envelope transmembrane protein (gp41) cytoplasmic domain (CD), we performed a yeast two-hybrid screen of a phytohemagglutinin-activated human T-cell cDNA library with the SIV gp41 CD. The majority of positive clones (50 of 54) encoded the prenylated Rabacceptor (PRA1). PRA1 is a 21-kDa protein associated with Golgi membranes that binds to prenylated Rab proteins in their GTP-bound state. While the cellular function of PRA1 is presently unknown, this protein appears to participate in intracellular vesicular trafficking, based on its cellular localization and ability to bind multiple members of the Rab protein family. Mammalian two-hybrid assays confirmed the interaction between the SIV gp41 CD and PRA1 Furthermore, gp41 sequences important for PRA1 binding were mappedto a central leucine-rich, amphipathic ct-helix in the SIV gp41 cytoplasmic tail. Although the human immunodeficiency virus (HIV-1) gp41 CD failed tointeract with PRA1 in the yeast two-hybrid system, its interaction with PRA1 was significantly better than that of the SIV gp41 CD in mammalian two-hybrid assays. Interestingly, PRA1 also interacted with the Env CDs of HIV-2, bovine immunodeficiency virus, equine infectious anemia virus, and felineimmunodeficiency virus. Thus, PRA1 associates with envelope glycoproteins from widely divergent lentiviruses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 11:38:52