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Titolo:
Enhancement of diphtheria toxin potency by replacement of the receptor binding domain with tetanus toxin C-fragment: A potential vector for delivering heterologous proteins to neurons
Autore:
Francis, JW; Brown, RH; Figueiredo, D; Remington, MP; Castillo, O; Schwarzschild, MA; Fishman, PS; Murphy, JR; vanderSpek, JC;
Indirizzi:
Massachusetts Gen Hosp, Cecil B Day Ctr Neuromuscular Res, Dept Neurol, Charlestown, MA 02129 USA Massachusetts Gen Hosp Charlestown MA USA 02129 Charlestown, MA 02129 USA Massachusetts Gen Hosp, Dept Neurol, Mol Neurobiol Lab, Charlestown, MA 02129 USA Massachusetts Gen Hosp Charlestown MA USA 02129 Charlestown, MA 02129 USA Harvard Univ, Sch Med, Charlestown, MA USA Harvard Univ Charlestown MA USA rvard Univ, Sch Med, Charlestown, MA USA Boston Univ, Sch Med, Dept Med, Boston, MA 02118 USA Boston Univ Boston MA USA 02118 , Sch Med, Dept Med, Boston, MA 02118 USA Univ Maryland, Sch Med, Dept Neurol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 Dept Neurol, Baltimore, MD 21201 USA Baltimore Vet Affairs Med Ctr, Res Serv, Baltimore, MD USA Baltimore Vet Affairs Med Ctr Baltimore MD USA s Serv, Baltimore, MD USA
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 6, volume: 74, anno: 2000,
pagine: 2528 - 2536
SICI:
0022-3042(200006)74:6<2528:EODTPB>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETROGRADE AXONAL-TRANSPORT; RAT-BRAIN MEMBRANES; GENETIC CONSTRUCTION; SUPEROXIDE-DISMUTASE; TARGETED DELIVERY; ESCHERICHIA-COLI; FUSION PROTEIN; CELL-LINE; TRANSLOCATION; EXPRESSION;
Keywords:
diphtheria toxin : tetanus toxin fusion protein; vector delivery system; neurons;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Francis, JW Massachusetts Gen Hosp, Cecil B Day Ctr Neuromuscular Res, Dept Neurol, Bldg 149,13th St,room 6627, Charlestown, MA 02129 USA Massachusetts Gen Hosp Bldg 149,13th St,room 6627 Charlestown MA USA 02129
Citazione:
J.W. Francis et al., "Enhancement of diphtheria toxin potency by replacement of the receptor binding domain with tetanus toxin C-fragment: A potential vector for delivering heterologous proteins to neurons", J NEUROCHEM, 74(6), 2000, pp. 2528-2536

Abstract

This study describes the expression, purification, and characterization ofa recombinant fusion toxin, DAB(389)TTC, composed of the catalytic and membrane translocation domains of diphtheria toxin (DAB(389)) linked to the receptor binding fragment of tetanus toxin (C-fragment). As determined by itsability to inhibit cellular protein synthesis in primary neuron cultures, DAB(389)TTC was similar to 1,000-fold more cytotoxic than native diphtheriatoxin or the previously described fusion toxin, DAB(389)MSH. The cytotoxiceffect of DAB(389)TTC on cultured cells was specific toward neuronal-type cells and was blocked by coincubation of the chimeric toxin with tetanus antitoxin. The toxicity of DAB(389)TTC, like that of diphtheria toxin, was dependent on passage through an acidic compartment and ADP-ribosyltransferaseactivity of the DAB(389) catalytic fragment. These results suggest that a catalytically inactive form of DAB(389)TTC may be useful as a nonviral vehicle to deliver exogenous proteins to the cytosolic compartment of neurons.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:19:45