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Titolo:
Canine adenovirus type 2 attachment and internalization: Coxsackievirus-adenovirus receptor, alternative receptors, and an RGD-independent pathway
Autore:
Soudais, C; Boutin, S; Hong, SS; Chillon, M; Danos, O; Bergelson, JM; Boulanger, P; Kremer, EJ;
Indirizzi:
Genethon III, CNRS, URA 1923, F-91002 Evry, France Genethon III Evry France F-91002 I, CNRS, URA 1923, F-91002 Evry, France CNRS, UMR 5537, Lab Virol & Pathogenese Virale, Lyon, France CNRS Lyon France UMR 5537, Lab Virol & Pathogenese Virale, Lyon, France Childrens Hosp Philadelphia, Div Immunol & Infect Dis, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 22, volume: 74, anno: 2000,
pagine: 10639 - 10649
SICI:
0022-538X(200011)74:22<10639:CAT2AA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN DENDRITIC CELLS; GENE DELIVERY; SUBGROUP-C; IN-VIVO; CELLULAR RECEPTORS; AIRWAY EPITHELIA; FIBER RECEPTOR; MELANOMA CELL; B VIRUSES; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Kremer, EJ Genethon III, CNRS, URA 1923, 1bis Rue Int, F-91002 Evry, France Genethon III 1bis Rue Int Evry France F-91002 002 Evry, France
Citazione:
C. Soudais et al., "Canine adenovirus type 2 attachment and internalization: Coxsackievirus-adenovirus receptor, alternative receptors, and an RGD-independent pathway", J VIROLOGY, 74(22), 2000, pp. 10639-10649

Abstract

The best-characterized receptors for adenoviruses (Ads) are the coxsackievirus-ad receptor (CAR) and integrins alpha (v)beta (5) and alpha (v)beta (3), which facilitate entry. The alpha (v) integrins recognize an Arg-Gly-Asp(RGD) motif found in some extracellular matrix proteins and in the penton base in most human Ads. Using a canine adenovirus type 2 (CAV-2) vector, wefound that CHO cells that express CAR but not wild-type CHO cells are susceptible to CAV-2 transduction. Cells expressing alpha (M)beta (2) integrinsor major histocompatibiIity complex class I (MHC-I) molecules but which donot express CAR were not transduced. Binding assays showed that CAV-2 attaches to a recombinant soluble form of CAR and that Ad type 5 (Ad5) fiber, penton base, and an anti-CAR antibody partially blocked attachment. Using fluorescently labeled CAV-2 particles, we found that in some cells nonpermissive for transduction, inhibition was at the point of internalization and not attachment. The transduction efficiency of CAV 2, which lacks an RGD motif, surprisingly mimicked that of Ad5 when tested in cells selectively expressing alpha (v)beta (5) and alpha (v)beta (3) integrins. Our results demonstrate that CAV-2 transduction is augmented by CAR and possibly by alpha (v)beta (5), though transduction can be CAR and alpha (v)beta (3/5) independent but is alpha (M)beta (2), MHC-I, and RGD independent, demonstrating a transduction mechanism which is distinct from that of Ad2/5.

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Documento generato il 02/07/20 alle ore 21:05:27