Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INCREASED INCORPORATION OF CHIMERIC HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GP120 PROTEINS INTO PR55(GAG) VIRUS-LIKE PARTICLES BY AN EPSTEIN-BARR-VIRUS GP220 350-DERIVED TRANSMEMBRANE DOMAIN/
Autore:
DEML L; KRATOCHWIL G; OSTERRIEDER N; KNUCHEL R; WOLF H; WAGNER R;
Indirizzi:
UNIV REGENSBURG,INST MED MICROBIOL,FRANZ JOSEF STR ALLEE 11 D-93053 REGENSBURG GERMANY UNIV REGENSBURG,INST MED MICROBIOL D-93053 REGENSBURG GERMANY UNIV REGENSBURG,INST PATHOL D-93053 REGENSBURG GERMANY UNIV MUNICH,INST MED MICRIOL INFECT & EPIDEM DIS D-80539 MUNICH GERMANY
Titolo Testata:
Virology
fascicolo: 1, volume: 235, anno: 1997,
pagine: 10 - 25
SICI:
0042-6822(1997)235:1<10:IIOCHT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT VACCINIA VIRUS; BACULOVIRUS-INFECTED CELLS; CYTOTOXIC T-LYMPHOCYTES; B SURFACE-ANTIGEN; ENVELOPE GLYCOPROTEIN; CYTOPLASMIC DOMAIN; INSECT CELLS; HIV-1 GAG; NEUTRALIZING ANTIBODIES; OLIGOMERIC STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
93
Recensione:
Indirizzi per estratti:
Citazione:
L. Deml et al., "INCREASED INCORPORATION OF CHIMERIC HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GP120 PROTEINS INTO PR55(GAG) VIRUS-LIKE PARTICLES BY AN EPSTEIN-BARR-VIRUS GP220 350-DERIVED TRANSMEMBRANE DOMAIN/", Virology, 235(1), 1997, pp. 10-25

Abstract

Noninfectious Pr55(gag) virus-like particles containing high quantities of oligomeric human immunodeficiency virus type-1 (HIV-1) envelope (Env) proteins represent potential candidate immunogens for a vaccine against HIV-1 infection. Thus, chimeric env genes were constructed encoding the HIV-1 exterior glycoprotein gp120 which was covalently linked at different C-terminal positions to a transmembrane domain (TM) from the Epstein-Barr virus (EBV) major Env glycoprotein gp220/ 350. All chimeric Env-TM polypeptides as well as the wild-type HIV Env proteinswere equally produced and incorporated the outer surface of insect cells using the baculovirus expression system. In the presence of coexpressed HIV pr55(gag) polyproteins significantly decreased amounts of wild-type Env proteins were presented al the cell surface, whereas the membrane incorporation of the Env-TM chimeras was not affected. Biochemical and immunoelectron microscopical analysis particles that were efficiently released from these cells displayed the incorporation of bothwild-type Env and chimeric Env-TM proteins on the surface of VLPs. However, the quantities of particle-associated chimeric Env-TM proteins exceeded those of incorporated wild-type Env proteins by a factor of 5-10. Chemical cross-linking and subsequent polyacrylamide gel electrophoresis of VLP-entrapped Env proteins revealed that the chimeric Env-TM proteins form homodimers and a higher-order oligomer, similar to that observed for wild-type Env proteins. Thus, the results of this studyclearly demonstrate that the replacement of the gp41 transmembrane protein of gp160 by a heterologous, EBV gp220/350-derived membrane anchor provides an effective strategy to incorporate high quantities of oligomeric HIV gp120 proteins on the surface of Pr55(gag) virus-like particles. (C) 1997 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 11:50:40