Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Tyrosines 60, 64, and 101 of Epstein-Barr virus LMP2A are not essential for blocking B cell signal transduction
Autore:
Swart, R; Fruehling, S; Longnecker, R;
Indirizzi:
Northwestern Univ, Sch Med, Dept Immunol Microbiol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 l Microbiol, Chicago, IL 60611 USA
Titolo Testata:
VIROLOGY
fascicolo: 2, volume: 263, anno: 1999,
pagine: 485 - 495
SICI:
0042-6822(19991025)263:2<485:T66A1O>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH TRANSFORMATION INVITRO; MEMBRANE-PROTEIN LMP2; LYMPHOCYTE INFECTION; MARMOSET LEUKOCYTES; BURKITT-LYMPHOMA; LATENCY; DOMAINS; GENE; IDENTIFICATION; REACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Longnecker, R 303 E Chicago Ave, Chicago, IL 60611 USA 303 E Chicago Ave Chicago IL USA 60611 hicago, IL 60611 USA
Citazione:
R. Swart et al., "Tyrosines 60, 64, and 101 of Epstein-Barr virus LMP2A are not essential for blocking B cell signal transduction", VIROLOGY, 263(2), 1999, pp. 485-495

Abstract

Epstein-Barr virus (EBV) latent membrane protein 2A (LM P2A) is expressed on the membrane of B-lymphocytes a nd blocks B cell receptor (BCR) signaling in EBV-transformed B-lymphocytes in vitro. The LMP2A amino-terminal domain, which is essential for the LMP2A-mediated block of B cell signal transduction, contains eight tyrosine residues. Three of these tyrosine residues (Y74, Y85, and Y112) have been demonstrated to be essential for the LMP2A-mediated block on protein tyrosine phosphorylation, calcium mobilization, andinduction of BZLF1 expression after BCR activation. To investigate the importance of tyrosines at positions 60, 64, and 101 on B cell signaling, EBV recombinants were constructed containing a tyrosine-to-phenylalanine point mutation at amino acid 60, 64, or 101 within LMP2A. Tyrosine phosphorylation, calcium mobilization, and induction of BZLF1 expression were not affected by any of the tyrosine point mutations after BCR activation. In addition,constitutive phosphorylation of LM P2A was unaffected by any of the tyrosine point mutations. These data indicate that tyrosines 60, 64, and 101 are not essential for the LMP2A-mediated block of B cell signal transduction intransformed cell lines. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 08:34:49