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Titolo:
Cellular uptake and nuclear delivery of recombinant adenovirus Penton base
Autore:
Hong, SS; Gay, B; Karayan, L; Dabauvalle, MC; Boulanger, P;
Indirizzi:
RTH Laennec, Fac Med, Lab Virol & Pathogenese Virale, CNRS UMR 5537, F-69008 Lyon, France RTH Laennec Lyon France F-69008 ale, CNRS UMR 5537, F-69008 Lyon, France Fac Med Montpellier, Inst Biol, Mol Virol Lab, F-34060 Montpellier, FranceFac Med Montpellier Montpellier France F-34060 34060 Montpellier, France Univ Wurzburg, Dept Cell & Dev Biol, Theodor Boveri Inst, D-97074 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97074 i Inst, D-97074 Wurzburg, Germany
Titolo Testata:
VIROLOGY
fascicolo: 1, volume: 262, anno: 1999,
pagine: 163 - 177
SICI:
0042-6822(19990915)262:1<163:CUANDO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; VIRUS TYPE-1 GAG; PORE COMPLEX; HELA-CELLS; SUBGROUP-C; NUCLEOCYTOPLASMIC TRANSPORT; ANTENNAPEDIA HOMEODOMAIN; GENE DELIVERY; EARLY EVENTS; 3RD HELIX;
Keywords:
adenovirus serotype 2 (Ad2); penton base; endocytosis; vesicular escape; nuclear import; nuclear pore complex; membrane translocation; protein trafficking;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
89
Recensione:
Indirizzi per estratti:
Indirizzo: Boulanger, P RTH Laennec, Fac Med, Lab Virol & Pathogenese Virale, CNRS UMR 5537, Rue Guillaume Paradin, F-69008 Lyon, France RTH Laennec Rue Guillaume Paradin Lyon France F-69008 France
Citazione:
S.S. Hong et al., "Cellular uptake and nuclear delivery of recombinant adenovirus Penton base", VIROLOGY, 262(1), 1999, pp. 163-177

Abstract

An Ad2 capsid component, the penton base, expressed as recombinant protein, was found to be capable of affecting the entire entry pathway of adenovirion in HeLa cells, i.e., cell attachment, endocytosis, vesicular escape, intracytoplasmic movement, and translocation through the nuclear pore complex. Data with pentamerization-defective mutants suggested that none of these successive steps depended upon penton base pentamer status, indicating thatthe peptide domains responsible for these functions were carried by the monomer. Observations performed with wild-type (WT) and an integrin-binding-site double-mutant (K288E340) suggested that the penton base could enter thecell via an alternative, RGD- and LDV-independent, pathway. Of three mutants that were found to be defective in nuclear addressing in insect cells, only one, W165H, was also altered in nuclear transport in HeLa cells. The other two, W119H and RRR547EQQ, showed a WT pattern of nuclear localization in HeLa cells, suggesting that the region including tryptophan-119 and the basic signal at position 547 did not act as a nuclear localization signal inthe human cell context. The integrity of cellular structures and the cytoskeleton seemed to be required for the vectorial movement and nuclear importof WT penton base, as suggested by experiments using permeabilized HeLa cells, isolated nuclear membranes, and cytoskeleton-targeted drugs. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 11:13:37