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Titolo:
INHIBITION OF HIV TYPE-1 INFECTIVITY BY COEXPRESSION OF A WILD-TYPE AND A DEFECTIVE GLYCOPROTEIN-120
Autore:
LUND OS; LOSMAN B; SCHONNING K; BOLMSTEDT A; OLOFSSON S; HANSEN JES;
Indirizzi:
UNIV COPENHAGEN,HVIDOVRE HOSP,DEPT 144,INFECT DIS LAB,KETTEGAARD ALLE30 DK-2650 HVIDOVRE DENMARK UNIV COPENHAGEN,HVIDOVRE HOSP,DEPT 144,INFECT DIS LAB DK-2650 HVIDOVRE DENMARK GOTHENBURG UNIV,DEPT CLIN VIROL S-41346 GOTHENBURG SWEDEN
Titolo Testata:
AIDS research and human retroviruses
fascicolo: 16, volume: 14, anno: 1998,
pagine: 1445 - 1450
SICI:
0889-2229(1998)14:16<1445:IOHTIB>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNODEFICIENCY-VIRUS TYPE-1; MEMBRANE-FUSION; CD4 RECEPTOR; T-CELLS; ENVELOPE; MUTANT; GP120; REPLICATION; EXPRESSION; INTERFERENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
O.S. Lund et al., "INHIBITION OF HIV TYPE-1 INFECTIVITY BY COEXPRESSION OF A WILD-TYPE AND A DEFECTIVE GLYCOPROTEIN-120", AIDS research and human retroviruses, 14(16), 1998, pp. 1445-1450

Abstract

An amino acid substitution (D --> K) in the C3 region of HIV-1 gp120 has previously been shown to inhibit binding of virions to CD4(+) cells. We have introduced the same mutation into the HIV-1 isolate LAV-I-BRU, in which the mutation is denoted D373K. Here we show that the D373K envelope protein is processed and incorporated into virus particles,but that D373K virions have no detectable infectivity (below 0.1% relative to wild type). When D373K and the wild-type envelope gene were cotransfected in 293 cells at a 4:1 ratio, the resultant infectivity ofthe HIV-1 supernatant was reduced more than 100-fold. When the same ratio of plasmids was tested in COS-1 cells the inhibition of HIV-1 wasan order of magnitude less than observed in 293 cells. COS-1 and 293 cells differed in that only 293 cells displayed saturation of virus production with respect to the envelope protein, Our data fit a simple model: when virion formation is saturated with envelope protein, expression and incorporation of a defective envelope protein imply a corresponding dilution of wild-type protein on the surface of virions. The cooperative function of wild-type envelope proteins is subsequently compromised, and a trans-dominant inhibition of virus infectivity is observed.

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Documento generato il 05/12/20 alle ore 23:59:10