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Titolo:
Negative factor from SIV binds to the catalytic subunit of the V-ATPase tointernalize CD4 and to increase viral infectivity
Autore:
Mandic, R; Fackler, OT; Geyer, M; Linnemann, T; Zheng, YH; Peterlin, BM;
Indirizzi:
Univ Calif San Francisco, Howard Hughes Med Inst, Dept Med, San Francisco,CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 rancisco,CA 94143 USA Univ Calif San Francisco, Howard Hughes Med Inst, Dept Microbiol & Immunol, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 ancisco, CA 94143 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 2, volume: 12, anno: 2001,
pagine: 463 - 473
SICI:
1059-1524(200102)12:2<463:NFFSBT>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIV-1 NEF PROTEIN; SIMIAN IMMUNODEFICIENCY VIRUS; CELL-SURFACE CD4; DOWN-REGULATION; CLATHRIN ADAPTER; DILEUCINE MOTIF; VACUOLAR (H+)-ATPASE; SORTING PATHWAYS; RHESUS MACAQUES; T-LYMPHOCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Peterlin, BM Univ Calif San Francisco, Howard Hughes Med Inst, Dept Med, San Francisco,CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 4143 USA
Citazione:
R. Mandic et al., "Negative factor from SIV binds to the catalytic subunit of the V-ATPase tointernalize CD4 and to increase viral infectivity", MOL BIOL CE, 12(2), 2001, pp. 463-473

Abstract

The accessory protein negative factor (Nef) from human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) is required for optimal viral infectivity and the progression to acquired immunodeficiency syndrome (AIDS). Nef interacts with the endocytic machinery, resulting in the down-regulation of cluster of differentiation antigen 4 (CD4) and major histocompatibility complex class I (MHCI) molecules on the surface of infected cells. Mutations in the C-terminal flexible loop of Nef result in a lower rate of internalization by this viral protein. However, no loop-dependent bindingof Nef to adaptor protein-2 (AP-2), which is the adaptor protein complex that is required for the internalization of proteins from the plasma membrane, could be demonstrated. In this study we investigated the relevance of different motifs in Nef from SIVmac239 for its internalization, CD4 down-regulation, binding to components of the trafficking machinery, and viral infectivity. Our data suggest that the binding of Nef to the catalytic subunit Hof the vacuolar membrane ATPase (V-ATPase) facilitates its internalization. This binding depends on the integrity of the whole flexible loop. Subsequent studies on Nef mutant viruses revealed that the flexible loop is essential for optimal viral infectivity. Therefore, our data demonstrate how Nef contacts the endocytic machinery in the absence of its direct binding to AP-2 and suggest an important role for subunit H of the V-ATPase in viral infectivity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 09:38:30