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Titolo:
ASSEMBLY AND EXTRACELLULAR RELEASE OF CHIMERIC HIV-1 PR55(GAG) RETROVIRUS-LIKE PARTICLES
Autore:
WAGNER R; DEML L; FLIESSBACH H; WANNER G; WOLF H;
Indirizzi:
KLINIKUM REGENSBURG,INST MED MIKROBIOL,FRANZ JOSEF STRAUSS ALLEE 11 D-93053 REGENSBURG GERMANY INST MED MIKROBIOL W-8400 REGENSBURG GERMANY LMU MUNCHEN,INST BOT MUNICH GERMANY
Titolo Testata:
Virology
fascicolo: 1, volume: 200, anno: 1994,
pagine: 162 - 175
SICI:
0042-6822(1994)200:1<162:AAEROC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; RECOMBINANT VACCINIA VIRUS; SURFACE-ANTIGEN PARTICLES; MURINE LEUKEMIA-VIRUS; MATRIX PROTEIN; SEROPOSITIVE INDIVIDUALS; MONOCLONAL-ANTIBODIES; INFECTION INVITRO; ENVELOPE PROTEIN; LYMPHOCYTE-T;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
59
Recensione:
Indirizzi per estratti:
Citazione:
R. Wagner et al., "ASSEMBLY AND EXTRACELLULAR RELEASE OF CHIMERIC HIV-1 PR55(GAG) RETROVIRUS-LIKE PARTICLES", Virology, 200(1), 1994, pp. 162-175

Abstract

The HIV-1 Pr55(gag) precursors were previously shown to assemble and bud from a variety of different cell types as noninfectious virus-likeparticles (VLPs) resembling immature HIV virions. The use of these VLPs as an immunogenic and autologous carrier component may allow the presentation of defined epitopes deduced from reading frames other than gag to the immune system, thereby avoiding the induction of adverse immune responses. In order to identify domains within Pr55(gag) that canbe replaced by immunologically relevant epitopes without affecting its capacity to assemble into VLPs, we deleted three domains of a predicted high surface probability. Deletion of amino acids 211-241 within p24CA and amino acids 436-471 within the p6LI portion of Pr55(gag) had no effect on the assembly, ultrastructure, biophysical properties, andyields of mutant VLPs when expressed via recombinant vaccinia virusesin mammalian cells. Deletion of amino acids 99-154 overlapping the p17MA/p24CA cleavage site completely abolished the capacity of the gag polyprotein to form VLPs and led to a reduction of immature Pr55 VLPs released into the cell-culture supernatants when coexpressed with wild-type Pr55(gag). In contrast, assembly and budding of chimeric VLPs could be demonstrated after replacing amino acids 211-241 and 436-471 by immunologically relevant epitopes derived from reading frames other than pr55(gag) (e.g., vs loop; CD4-binding-domain; nef-CTL epitope) or after fusion of these sequences to the carboxy terminus of Pr55(gag). The importance of these data for the development of novel HIV candidatevaccines is discussed. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 01:28:38