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Titolo:
EXPRESSION AND CHARACTERIZATION OF CD4-IGG(2), A NOVEL HETEROTETRAMERTHAT NEUTRALIZES PRIMARY HIV TYPE-1 ISOLATES
Autore:
ALLAWAY GP; DAVISBRUNO KL; BEAUDRY GA; GARCIA EB; WONG EL; RYDER AM; HASEL KW; GAUDUIN MC; KOUP RA; MCDOUGAL JS; MADDON PJ;
Indirizzi:
PROGEN PHARMACEUT INC,777 OLD SAW MILL RIVER RD TARRYTOWN NY 10591 AARON DIAMOND AIDS RES CTR NEW YORK NY 10016 CTR DIS CONTROL & PREVENT ATLANTA GA 30333
Titolo Testata:
AIDS research and human retroviruses
fascicolo: 5, volume: 11, anno: 1995,
pagine: 533 - 539
SICI:
0889-2229(1995)11:5<533:EACOCA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT SOLUBLE CD4; INFECTION; VIRUS; MOLECULES; GP120; DISSOCIATION; INHIBITION; ANTIBODIES; VIRIONS; FUSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
G.P. Allaway et al., "EXPRESSION AND CHARACTERIZATION OF CD4-IGG(2), A NOVEL HETEROTETRAMERTHAT NEUTRALIZES PRIMARY HIV TYPE-1 ISOLATES", AIDS research and human retroviruses, 11(5), 1995, pp. 533-539

Abstract

CD4-IgG(2) is a novel fusion protein comprising human IgG(2) in whichthe Fv portions of both heavy and light chains have been replaced by the V1 and V2 domains of human CD4. This tetrameric protein is being developed as an immunoprophylactic agent to reduce the probability of infection following HIV-1 exposure, in settings such as occupational orperinatal exposure to the virus. CD4-IgG(2) has been expressed in Chinese hamster ovary cells and is secreted as a fully assembled heterotetramer. The protein binds with nanomolar affinity to purified gp120 from both a laboratory-adapted strain and a primary isolate of HIV-1. Pharmacokinetic studies in rabbits demonstrated that CD4-IgG(2) has a plasma terminal half-life greater than 1 day, compared with 15 min for soluble CD4 (sCD4), CD4-IgG(2) does not bind to Fc receptors on the surface of U937 monocyte/macrophage cells, Compared to molecules that incorporate the Fc portion of IgG(1), CD4-IgG(2) has less potential to mediate functions such as antibody-dependent enhancement of infection ortransplacental transmission of HIV-1. When tested in a virus-free HIV-1 envelope glycoprotein-mediated cell fusion assay, the tetrameric CD4-IgG(2) molecule inhibited syncytium formation more effectively than monomeric sCD4 or a dimeric CD4-gamma 2 fusion protein, This suggests the protein will block cell-to-cell transmission of HIV-1, Moreover, CD4-IgG(2) effectively neutralized a panel of laboratory-adapted strains and primary isolates of HIV-1, including strains with different tropisms and isolated from different stages of the disease, at concentrations that should be readily achieved in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 19:28:27