Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
AN INTEGRAL MEMBRANE-PROTEIN (LMP2) BLOCKS REACTIVATION OF EPSTEIN-BARR-VIRUS FROM LATENCY FOLLOWING SURFACE-IMMUNOGLOBULIN CROSS-LINKING
Autore:
MILLER CL; LEE JH; KIEFF E; LONGNECKER R;
Indirizzi:
HARVARD UNIV,SCH MED,DEPT MED,75 FRANCIS ST BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT MED BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT MICROBIOL & MOLEC GENET BOSTON MA 02115
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 2, volume: 91, anno: 1994,
pagine: 772 - 776
SICI:
0027-8424(1994)91:2<772:AIM(BR>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
BURKITT-LYMPHOMA; IMMORTALIZED LYMPHOCYTES; MARMOSET LEUKOCYTES; TYROSINE KINASE; TRANSFORMATION; CELLS; EXPRESSION; ACTIVATION; INFECTION; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
C.L. Miller et al., "AN INTEGRAL MEMBRANE-PROTEIN (LMP2) BLOCKS REACTIVATION OF EPSTEIN-BARR-VIRUS FROM LATENCY FOLLOWING SURFACE-IMMUNOGLOBULIN CROSS-LINKING", Proceedings of the National Academy of Sciences of the United Statesof America, 91(2), 1994, pp. 772-776

Abstract

The role of latent membrane protein 2 (LMP2) in Epstein-Barr virus (EBV) infection was evaluated by using latently infected primary B lymphocytes that had been growth transformed by wild-type or specifically mutated EBV recombinants. LMP2 null mutant recombinant EBV-infected cells were similar to normal B lymphocytes in their rapid increase in intracellular free calcium after surface immunoglobulin crosslinking. These cells also became more permissive for lytic EBV replication. In sharp contrast, wild-type control infected cells had little or no increase in intracellular free calcium or in permissivity For EBV replication. The block to surface immunoglobulin crosslinking induced permissivity in cells expressing wild-type LMP2 could be bypassed by raising intracellular free calcium levels with an ionophore and by activating protein kinase C with phorbol 12-myristate 13-acetate. LMP2A, not LMP2B, mediates this effect on calcium mobilization. Genetic and biochemical data are consistent with these effects being due to the interaction of the LMP2A N-terminal cytoplasmic domain with B lymphocyte src family tyrosine kinases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:02:53